| General information | | DisProt: | DP00701 | | Name: | Anti sigma factor FlgM | | Synonym(s): | O66683_AQUAE
FlgM
| | First appeared in release: | Release 5.5 (11/17/2010) | | UniProt: | O66683 | | UniGene: | | | SwissProt: | O66683_AQUAE | | TrEMBL: | | | NCBI (GI): | | | Source organism: | Aquifex aeolicus | | Sequence length: | 88 | | Percent disordered: | 94% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MVNRIELSRL IGLLLETEKR KNTEQKESGT NKIEDKVTLS KIAQELSKND VEEKDLEKKV - 60
KELKEKIEKG EYEVSDEKVV KGLIEFFT
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| Functional narrative |
It is hypothesized that FlgM functions similarly in A. aeolicus as it does in a different organism: Salmonella typhimurium. In S. typhimurium, FlgM functions as a negative regulator of flagella and chemotaxis genes. The FlgM protein binds to the σ28 protein, inhibiting transcription of Class 3 (or late-stage) genes until the basal body-hook body structure that forms the base of the flagella is properly assembled. Once the basal body-hook body structure is properly assembled, FlgM is exported from the cell allowing σ28 to initiate transcription of the Class 3 genes. (Molloy)
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered w/ Residual Structure | | Name: | H1 | | Location: | 5 - 17 | | Length: | 13 | | Region sequence: |
IELSRLIGLLLET | | Modification type: | Complex
Native
| | PDB: | 1RP3:B, 1SC5:B | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein inhibitor
Protein-protein binding
Intraprotein interaction
| Detection methods:
- X-ray crystallography (277 K; pH: 6.5; PEG 8000 16.2 %; Sodium cacodylate 0.09 M; Calcium acetate 0.18 M; Isopropanol 3 %)
- Circular dichroism (CD) spectroscopy, far-UV (358 K; pH: 7.4; Sodium phosphate 10 nM)
- Fluorescent probes (298 K; FlAsH binding buffer (10mM HEPES, 1mM TCEP, 1mM BME) 40 nM; FlgM 0.1 uM)
| References:
- Molloy RG, Ma WK, Allen AC, Greenwood K, Bryan L, Sacora R, Williams L, Gage MJ. "Aquifex aeolicus FlgM protein exhibits a temperature-dependent disordered nature." Biochim. Biophys. Acta. 2010; 1804(7): 1457-66. PubMed: 20298817
- Sorenson MK, Ray SS, Darst SA. "Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation." Mol. Cell. 2004; 14(1): 127-38. PubMed: 15068809
| Comments:According to Molloy et al (2010), fluorescent probe experiments suggest that for unbound FlgM at room temperature, helices 1 and 2 self-associate.
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| Region 2 | | Type: | Disordered | | Name: | linker | | Location: | 18 - 30 | | Length: | 13 | | Region sequence: |
EKRKNTEQKESGT | | Modification type: | Complex
Native
| | PDB: | 1RP3:B, 1SC5:B | | Structural/functional type: | Function arises from the disordered state
Relationship to function unknown
| | Functional classes: | Entropic chain
| | Functional subclasses: | Flexible linkers/spacers
| Detection methods:
- X-ray crystallography (277 K; pH: 6.5; Calcium acetate 0.18 M; Isopropanol 3 %; PEG 8000 16.2 %; Sodium cacodylate 0.09 M)
- Circular dichroism (CD) spectroscopy, far-UV (358 K; pH: 7.4; Sodium phosphate 10 mM)
| References:
- Molloy RG, Ma WK, Allen AC, Greenwood K, Bryan L, Sacora R, Williams L, Gage MJ. "Aquifex aeolicus FlgM protein exhibits a temperature-dependent disordered nature." Biochim. Biophys. Acta. 2010; 1804(7): 1457-66. PubMed: 20298817
- Sorenson MK, Ray SS, Darst SA. "Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation." Mol. Cell. 2004; 14(1): 127-38. PubMed: 15068809
| Comments:
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| Region 3 | | Type: | Disordered w/ Residual Structure | | Name: | H2 | | Location: | 31 - 46 | | Length: | 16 | | Region sequence: |
NKIEDKVTLSKIAQEL | | Modification type: | Complex
Native
| | PDB: | 1RP3:B, 1SC5:B | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Intraprotein interaction
Protein inhibitor
Protein-protein binding
| Detection methods:
- X-ray crystallography (277 K; pH: 6.5; Calcium acetate 0.18 M; Isopropanol 3 %; PEG 8000 16.2 %; Sodium cacodylate 0.09 M)
- Circular dichroism (CD) spectroscopy, far-UV (358 K; pH: 7.4; Sodium phosphate 10 mM)
- Fluorescent probes (298 K; FlAsH binding buffer (10mM HEPES, 1mM TCEP, 1mM BME) 40 nM; FlgM 0.1 uM)
| References:
- Molloy RG, Ma WK, Allen AC, Greenwood K, Bryan L, Sacora R, Williams L, Gage MJ. "Aquifex aeolicus FlgM protein exhibits a temperature-dependent disordered nature." Biochim. Biophys. Acta. 2010; 1804(7): 1457-66. PubMed: 20298817
- Sorenson MK, Ray SS, Darst SA. "Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation." Mol. Cell. 2004; 14(1): 127-38. PubMed: 15068809
| Comments:According to Molloy et al (2010), fluorescent probe experiments suggest that for unbound FlgM at room temperature, helices 1 and 2 self-associate.
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| Region 4 | | Type: | Disordered | | Name: | linker | | Location: | 47 - 55 | | Length: | 9 | | Region sequence: |
SKNDVEEKD | | Modification type: | Complex
Native
| | PDB: | 1RP3:B, 1SC5:B | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Entropic chain
| | Functional subclasses: | Flexible linkers/spacers
| Detection methods:
- X-ray crystallography (277 K; pH: 6.5; Calcium acetate 0.18 M; Isopropanol 3 %; PEG 8000 16.2 %; Sodium cacodylate 0.09 M)
- Circular dichroism (CD) spectroscopy, far-UV (358 K; pH: 7.4; Sodium phosphate 10 nM)
| References:
- Molloy RG, Ma WK, Allen AC, Greenwood K, Bryan L, Sacora R, Williams L, Gage MJ. "Aquifex aeolicus FlgM protein exhibits a temperature-dependent disordered nature." Biochim. Biophys. Acta. 2010; 1804(7): 1457-66. PubMed: 20298817
- Sorenson MK, Ray SS, Darst SA. "Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation." Mol. Cell. 2004; 14(1): 127-38. PubMed: 15068809
| Comments:
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| Region 5 | | Type: | Disordered w/ Residual Structure | | Name: | H3 | | Location: | 56 - 68 | | Length: | 13 | | Region sequence: |
LEKKVKELKEKIE | | Modification type: | Complex
Native
| | PDB: | 1RP3:B, 1SC5:B | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein inhibitor
| Detection methods:
- X-ray crystallography (277 K; pH: 6.5; Calcium acetate 0.18 M; Isopropanol 3 %; PEG 8000 16.2 %; Sodium cacodylate 0.09 M)
- Circular dichroism (CD) spectroscopy, far-UV (pH: 7.4; Sodium phosphate 10 nM)
| References:
- Molloy RG, Ma WK, Allen AC, Greenwood K, Bryan L, Sacora R, Williams L, Gage MJ. "Aquifex aeolicus FlgM protein exhibits a temperature-dependent disordered nature." Biochim. Biophys. Acta. 2010; 1804(7): 1457-66. PubMed: 20298817
- Sorenson MK, Ray SS, Darst SA. "Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation." Mol. Cell. 2004; 14(1): 127-38. PubMed: 15068809
| Comments:
|
| Region 6 | | Type: | Disordered | | Name: | linker | | Location: | 69 - 75 | | Length: | 7 | | Region sequence: |
KGEYEVS | | Modification type: | Complex
Native
| | PDB: | 1RP3:B, 1SC5:B | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Entropic chain
| | Functional subclasses: | Flexible linkers/spacers
| Detection methods:
- X-ray crystallography (277 K; pH: 6.5; Calcium acetate 0.18 M; Isopropanol 3 %; PEG 8000 16.2 %; Sodium cacodylate 0.09 M)
- Circular dichroism (CD) spectroscopy, far-UV (358 K; pH: 7.4; Sodium phosphate 10 nM)
| References:
- Molloy RG, Ma WK, Allen AC, Greenwood K, Bryan L, Sacora R, Williams L, Gage MJ. "Aquifex aeolicus FlgM protein exhibits a temperature-dependent disordered nature." Biochim. Biophys. Acta. 2010; 1804(7): 1457-66. PubMed: 20298817
- Sorenson MK, Ray SS, Darst SA. "Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation." Mol. Cell. 2004; 14(1): 127-38. PubMed: 15068809
| Comments:
|
| Region 7 | | Type: | Disordered w/ Residual Structure | | Name: | H4 | | Location: | 76 - 87 | | Length: | 12 | | Region sequence: |
DEKVVKGLIEFF | | Modification type: | Complex
Native
| | PDB: | 1RP3:B, 1SC5:B | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein inhibitor
| Detection methods:
- X-ray crystallography (277 K; pH: 6.5; Calcium acetate 0.18 M; Isopropanol 3 %; PEG 8000 16.2 %; Sodium cacodylate 0.09 M)
- Circular dichroism (CD) spectroscopy, far-UV (358 K; pH: 7.4; Sodium phosphate 10 nM)
| References:
- Molloy RG, Ma WK, Allen AC, Greenwood K, Bryan L, Sacora R, Williams L, Gage MJ. "Aquifex aeolicus FlgM protein exhibits a temperature-dependent disordered nature." Biochim. Biophys. Acta. 2010; 1804(7): 1457-66. PubMed: 20298817
- Sorenson MK, Ray SS, Darst SA. "Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation." Mol. Cell. 2004; 14(1): 127-38. PubMed: 15068809
| Comments:
|
| References |
- Molloy RG, Ma WK, Allen AC, Greenwood K, Bryan L, Sacora R, Williams L, Gage MJ. "Aquifex aeolicus FlgM protein exhibits a temperature-dependent disordered nature." Biochim. Biophys. Acta. 2010; 1804(7): 1457-66. PubMed: 20298817
- Sorenson MK, Ray SS, Darst SA. "Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation." Mol. Cell. 2004; 14(1): 127-38. PubMed: 15068809
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| Comments |
PDB structures (x-ray crystallography) are from Sorensen et al (2004), and show anti-sigma factor FlgM in complex with flagellar sigma-28. Circular dichroism and fluorescent probe experiments were performed by Molloy et al (2010).
The Sorensen et al (2004) cyrstallography was produced at 277K, a non-physiological temperature for this thermophilic organism. Molloy et al (2010) included CD experiments at 358K (approximating the physiological temperature) that showed more disordered-extended conformation than Sorensen, but still retained substantial residual alpha-helical character.
[Author Verified: 11/12/2010 PubMed 20298817]
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