General information | DisProt: | DP00741 | Name: | Regulatory protein cro | Synonym(s): | RCRO_LAMBD
lambda Cro
| First appeared in release: | Release 6.01 (10/15/2012) | UniProt: | P03040 | UniGene: | | SwissProt: | RCRO_LAMBD | TrEMBL: | | NCBI (GI): | | Source organism: | Enterobacteria phage lambda | Sequence length: | 66 | Percent disordered: | 8% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MEQRITLKDY AMRFGQTKTA KDLGVYQSAI NKAIHAGRKI FLTINADGSV YAEEVKPFPS - 60 NKKTTA
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Functional narrative |
Cro represses genes normally expressed in early phage development and is necessary for the late stage of lytic growth. It does this by binding to the OL and OR operators regions normally used by the repressor protein for lysogenic maintenance. Binds DNA as a homodimer.
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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: | Ordered | Name: | N-terminal | Location: | 1 - 2 | Length: | 2 | Region sequence: |
ME | Modification type: | Complex
Native
| PDB: | 1COP:D, 4CRO:A, 5CRO:A, 6CRO:A | Structural/functional type: | | Functional classes: | | Functional subclasses: | | Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 6.4; lambda Cro, native (PDB 1COP))
- X-ray crystallography (pH: 6.9; DNA fragment (in complex); lambda Cro (PDB 4CRO); Na cacodylate; NaCl)
- X-ray crystallography (293 K; pH: 6.9; Ammonium sulfate 70 mM; DNA fragment (in complex); lambda Cro (PDB 6CRO); Na cacodylate 20 mM; PEG 3350 13 %)
- X-ray crystallography (290 K; pH: 7.5; lambda Cro (PDB 5CRO); phospate 1.2 M)
| References:
- Albright RA, Matthews BW. "Crystal structure of lambda-Cro bound to a consensus operator at 3.0 A resolution." J. Mol. Biol.. 1998; 280(1): 137-51. PubMed: 9653037
- Anderson WF, Ohlendorf DH, Takeda Y, Matthews BW. "Structure of the cro repressor from bacteriophage lambda and its interaction with DNA." Nature. 1981; 290(5809): 754-8. PubMed: 6452580
- Brennan RG, Roderick SL, Takeda Y, Matthews BW. "Protein-DNA conformational changes in the crystal structure of a lambda Cro-operator complex." Proc. Natl. Acad. Sci. U.S.A.. 1990; 87(20): 8165-9. PubMed: 2146682
- Matsuo H, Shirakawa M, Kyogoku Y. "Three-dimensional dimer structure of the lambda-Cro repressor in solution as determined by heteronuclear multidimensional NMR." J. Mol. Biol.. 1995; 254(4): 668-80. PubMed: 7500341
- Ohlendorf DH, Tronrud DE, Matthews BW. "Refined structure of Cro repressor protein from bacteriophage lambda suggests both flexibility and plasticity." J. Mol. Biol.. 1998; 280(1): 129-36. PubMed: 9653036
| Comments:Structure references are as follows:
PDB 1COP is from Matsuo et al, 1995;
PDB 4CRO is from Anderson et al, 1981 and Brennan et al, 1990;
PDB 5CRO is from Ohlendorf et al, 1998;
PDB 6CRO is from Albright et al, 1998 and Ohlendorf et al, 1998.
Region 1 is considered disordered by some, but according to author BW Matthews, is easily visible in 5CRO and therefore "essentially ordered."
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Region 2 | Type: | Ordered | Name: | flexible hydrophobic core | Location: | 3 - 61 | Length: | 59 | Region sequence: |
QRITLKDYAMRFGQTKTAKDLGVYQSAINKAIHAGRKIFLTINADGSVYAEEVKPFPSN | Modification type: | Complex
Native
| PDB: | 1COP:D, 4CRO:A, 5CRO:A, 6CRO:A | Structural/functional type: | Function arises from the ordered state | Functional classes: | Molecular recognition effectors
| Functional subclasses: | Intraprotein interaction
DNA bending
Protein-DNA binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 6.4; lambda Cro, native (PDB 1COP))
- X-ray crystallography (pH: 6.9; DNA fragment (in complex); lambda Cro (PDB 4CRO); Na cacodylate; NaCl)
- X-ray crystallography (293 K; pH: 6.9; Ammonium sulfate 70 mM; DNA fragment (in complex); lambda Cro (PDB 6CRO); Na cacodylate 20 mM; PEG 3350 13 %)
- X-ray crystallography (290 K; pH: 7.5; lambda Cro (PDB 5CRO); phospate 1.2 M)
| References:
- Albright RA, Matthews BW. "Crystal structure of lambda-Cro bound to a consensus operator at 3.0 A resolution." J. Mol. Biol.. 1998; 280(1): 137-51. PubMed: 9653037
- Anderson WF, Ohlendorf DH, Takeda Y, Matthews BW. "Structure of the cro repressor from bacteriophage lambda and its interaction with DNA." Nature. 1981; 290(5809): 754-8. PubMed: 6452580
- Brennan RG, Roderick SL, Takeda Y, Matthews BW. "Protein-DNA conformational changes in the crystal structure of a lambda Cro-operator complex." Proc. Natl. Acad. Sci. U.S.A.. 1990; 87(20): 8165-9. PubMed: 2146682
- Matsuo H, Shirakawa M, Kyogoku Y. "Three-dimensional dimer structure of the lambda-Cro repressor in solution as determined by heteronuclear multidimensional NMR." J. Mol. Biol.. 1995; 254(4): 668-80. PubMed: 7500341
- Ohlendorf DH, Tronrud DE, Matthews BW. "Refined structure of Cro repressor protein from bacteriophage lambda suggests both flexibility and plasticity." J. Mol. Biol.. 1998; 280(1): 129-36. PubMed: 9653036
| Comments:Structure references are as follows:
PDB 1COP is from Matsuo et al, 1995;
PDB 4CRO is from Anderson et al, 1981 and Brennan et al, 1990;
PDB 5CRO is from Ohlendorf et al, 1998;
PDB 6CRO is from Albright et al, 1998 and Ohlendorf et al, 1998.
All references were consistent in their descriptions of this region being flexible and changing conformations upon DNA binding, summarized by Albright et al (1998) this way, "Compared to the crystal structure of free Cro, the Cro dimer undergoes substantial changes in conformation on binding operator, including both interdomain hinge-bending, and changes within each subunit that widen the channel occupied by the DNA backbone. Dimer flexibility, therefore, appears to be important for Cro function. Furthermore, the central b-sheet region of the dimer, better described as a series of slightly overlapping anti-parallel b-ribbons, appears designed to permit flexibility."
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Region 3 | Type: | Disordered | Name: | C-terminal | Location: | 62 - 66 | Length: | 5 | Region sequence: |
KKTTA | Modification type: | Complex
| PDB: | 1COP:D, 4CRO:A, 5CRO:A, 6CRO:A | Structural/functional type: | Function arises from the disordered state | Functional classes: | Molecular recognition effectors
Molecular assembly
| Functional subclasses: | Intraprotein interaction
DNA bending
Protein-DNA binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 6.4; lambda Cro, native (PDB 1COP))
- X-ray crystallography (pH: 6.9; DNA fragment (in complex); lambda Cro (PDB 4CRO); Na cacodylate; NaCl)
- X-ray crystallography (293 K; pH: 6.9; Ammonium sulfate 70 mM; DNA fragment (in complex); lambda Cro (PDB 6CRO); Na cacodylate 20 mM; PEG 3350 13 %)
- X-ray crystallography (290 K; pH: 7.5; lambda Cro (PDB 5CRO); phospate 1.2 M)
| References:
- Albright RA, Matthews BW. "Crystal structure of lambda-Cro bound to a consensus operator at 3.0 A resolution." J. Mol. Biol.. 1998; 280(1): 137-51. PubMed: 9653037
- Anderson WF, Ohlendorf DH, Takeda Y, Matthews BW. "Structure of the cro repressor from bacteriophage lambda and its interaction with DNA." Nature. 1981; 290(5809): 754-8. PubMed: 6452580
- Brennan RG, Roderick SL, Takeda Y, Matthews BW. "Protein-DNA conformational changes in the crystal structure of a lambda Cro-operator complex." Proc. Natl. Acad. Sci. U.S.A.. 1990; 87(20): 8165-9. PubMed: 2146682
- Matsuo H, Shirakawa M, Kyogoku Y. "Three-dimensional dimer structure of the lambda-Cro repressor in solution as determined by heteronuclear multidimensional NMR." J. Mol. Biol.. 1995; 254(4): 668-80. PubMed: 7500341
- Ohlendorf DH, Tronrud DE, Matthews BW. "Refined structure of Cro repressor protein from bacteriophage lambda suggests both flexibility and plasticity." J. Mol. Biol.. 1998; 280(1): 129-36. PubMed: 9653036
| Comments:Structure references are as follows:
PDB 1COP is from Matsuo et al, 1995;
PDB 4CRO is from Anderson et al, 1981 and Brennan et al, 1990;
PDB 5CRO is from Ohlendorf et al, 1998;
PDB 6CRO is from Albright et al, 1998 and Ohlendorf et al, 1998.
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Comments |
AV sent 10/3/2012 (PMID 9653036)
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