General information | DisProt: | DP00703 | Name: | Teg12 | Synonym(s): | B7T1D7_9BACT
Teicoplanin-like eDNA-derived gene cluster
| First appeared in release: | Release 5.6 (01/10/2011) | UniProt: | B7T1D7 | UniGene: | | SwissProt: | B7T1D7_9BACT | TrEMBL: | | NCBI (GI): | | Source organism: | uncultured soil bacterium | Sequence length: | 285 | Percent disordered: | 19% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MNGIRWIASY PKAGNTWVRC MLAAYITGKA PQVWNDIDAE SLTLEAMLRF GDLPPAEPME - 60 PVLVKTHLKA DVPVLGLYGE ATAKVLYLVR NPRDMLLSSM RMASISRDDV EKSRDFARKF - 120 IANEGLGWNA LGAGGGVGLG SWPENVRSWT ESSSDRFPNA DVLTMRYEDL KGDPVARFSE - 180 IVEFLDLGGP VDIEDIRRAV AASTLERMRE LEKRSEQQGG GSPIRHGDAR MMKGGPGGAR - 240 PQFVGEGRYD QSLSFLGEDI ESDYQELLHG DSGFALYAKQ YGYAG
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Functional narrative |
Molecular function inferred as sulfotransferase activity. (UniProt/InterPro)
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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 | Name: | Variable region 1 (V1) loop | Location: | 37 - 43 | Length: | 7 | Region sequence: |
IDAESLT | Modification type: | Native
| PDB: | 3MG9:A, 3MGB:A, 3MGC:A | Structural/functional type: | Relationship to function unknown | Functional classes: | Molecular assembly
| Functional subclasses: | Sulfation
| Detection methods:
- X-ray crystallography (295 K; pH: 6.5; protein (1:1 uL concentration to crystallation soln) 7.5 mg/mL; Sodium Citrate 1 M; Sodium Cacodylate 0.1 M; Silver Bullet Reagent 29 ((Hampton)))
| References:
- Bick MJ, Banik JJ, Darst SA, Brady SF. "Crystal structures of the glycopeptide sulfotransferase Teg12 in a complex with the teicoplanin aglycone." Biochemistry. 2010; 49(19): 4159-68. PubMed: 20361791
| Comments:Bick et al (2010) report that in the Teg12-apo structure, V1 was an ordered alpha-helix in monomer A but disordered in monomer B.
Bick et al (2010) produced three crystal structures: Teg12-apo (PDB 3MGC), Teg12 binary complex with Teicoplanin Aglycone (PDB 3MG9) and Teg12 ternary complex with PAP and Teicoplanin Aglycone (PDB 3MGB).
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Region 2 | Type: | Disordered - Extended | Name: | Variable region 2 (V2) loop | Location: | 127 - 137 | Length: | 11 | Region sequence: |
GWNALGAGGGV | Modification type: | Native
| PDB: | 3MG9:A, 3MGB:A, 3MGC:A | Structural/functional type: | Function arises via a disorder to order transition | Functional classes: | Molecular assembly
| Functional subclasses: | Sulfation
| Detection methods:
- X-ray crystallography (295 K; pH: 6.5; protein (1:1 uL concentration to crystallation soln) 7.5 mg/mL; Silver Bullet Reagent 29 ((Hampton)); Sodium Cacodylate 0.1 M; Sodium Citrate 1 M)
| References:
- Bick MJ, Banik JJ, Darst SA, Brady SF. "Crystal structures of the glycopeptide sulfotransferase Teg12 in a complex with the teicoplanin aglycone." Biochemistry. 2010; 49(19): 4159-68. PubMed: 20361791
| Comments:Bick et al (2010) produced three crystal structures: Teg12-apo (PDB 3MGC), Teg12 binary complex with Teicoplanin Aglycone (PDB 3MG9) and Teg12 ternary complex with PAP and Teicoplanin Aglycone (PDB 3MGB).
According to Bick et al (2010, V2 was primarily disordered in the apo and binary strcutures, but full ordered in the ternary structure. The ternary structure also showed stabilization via aa 134 in V2 stacking with aa 223 of V3.
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Region 3 | Type: | Ordered | Name: | flexible GHL helix | Location: | 204 - 215 | Length: | 12 | Region sequence: |
TLERMRELEKRS | Modification type: | Native
| PDB: | 3MG9:A, 3MGB:A, 3MGC:A | Structural/functional type: | Function arises from the ordered state | Functional classes: | Molecular assembly
| Functional subclasses: | Sulfation
| Detection methods:
- X-ray crystallography (295 K; pH: 6.5; protein (1:1 uL concentration to crystallation soln) 7.5 mg/mL; Silver Bullet Reagent 29 ((Hampton)); Sodium Cacodylate 0.1 M; Sodium Citrate 1 M)
| References:
- Bick MJ, Banik JJ, Darst SA, Brady SF. "Crystal structures of the glycopeptide sulfotransferase Teg12 in a complex with the teicoplanin aglycone." Biochemistry. 2010; 49(19): 4159-68. PubMed: 20361791
| Comments:Bick et al (2010) produced three crystal structures: Teg12-apo (PDB 3MGC), Teg12 binary complex with Teicoplanin Aglycone (PDB 3MG9) and Teg12 ternary complex with PAP and Teicoplanin Aglycone (PDB 3MGB).
Bick et al (2010) so named the flexible GHL (glycopeptide-helix-loop) helix because of its important interactions with its neighboring loop and with glycopeptides. The back of the glycopeptide binding pocket is formed by aa 214 of the GHL helix and aa 248 of the V3 loop. Additional residues (206, 207, 210, 213) form contacts with glycopeptide.
The flexible nature of this helix also allows concurrent interactions of Teg12 with both glycopeptide and PAP.
In the ternary structure, GHL helix forms one contiguous helix with the alpha-helix at aa 193-203. In the apo and binary structures, GHL helix bends dramatically at aa 204.
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Region 4 | Type: | Disordered - Extended | Name: | Variable region 3 (V3) loop | Location: | 216 - 250 | Length: | 35 | Region sequence: |
EQQGGGSPIRHGDARMMKGGPGGARPQFVGEGRYD | Modification type: | Native
| PDB: | 3MG9:A, 3MGB:A, 3MGC:A | Structural/functional type: | Function arises from the disordered state | Functional classes: | Molecular assembly
| Functional subclasses: | Sulfation
| Detection methods:
- X-ray crystallography (295 K; pH: 6.5; protein (1:1 uL concentration to crystallation soln) 7.5 mg/mL; Silver Bullet Reagent 29 ((Hampton)); Sodium Cacodylate 0.1 M; Sodium Citrate 1 M)
| References:
- Bick MJ, Banik JJ, Darst SA, Brady SF. "Crystal structures of the glycopeptide sulfotransferase Teg12 in a complex with the teicoplanin aglycone." Biochemistry. 2010; 49(19): 4159-68. PubMed: 20361791
| Comments:Bick et al (2010) produced three crystal structures: Teg12-apo (PDB 3MGC), Teg12 binary complex with Teicoplanin Aglycone (PDB 3MG9) and Teg12 ternary complex with PAP and Teicoplanin Aglycone (PDB 3MGB).
Bick et al (2010) determined that flexible loop V3 (the "L" referred to in GHL, see Region 3) is important in binding both glycopeptide (at aa 225-242) and PAP (at aa 243-247). In Teg12, the back of the glycopeptide binding pocket is formed by aa 248 of V3 and 214 of GHL helix. In the ternary structure, it appears that aa 233 extends into the glycopeptide. Additionally, aa 223 stacks with aa 134 of the V2 segment to stabilize the structure.
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Region 5 | Type: | Disordered | Name: | GHL hinge | Location: | 204 - 204 | Length: | 1 | Region sequence: |
T | Modification type: | Native
| PDB: | 3MG9:A, 3MGB:A, 3MGC:A | Structural/functional type: | Function arises from the disordered state | Functional classes: | Entropic chain
| Functional subclasses: | Flexible linkers/spacers
| Detection methods:
- X-ray crystallography (295 K; pH: 6.5; protein (1:1 uL concentration to crystallation soln) 7.5 mg/mL; Silver Bullet Reagent 29 ((Hampton)); Sodium Cacodylate 0.1 M; Sodium Citrate 1 M)
| References:
- Bick MJ, Banik JJ, Darst SA, Brady SF. "Crystal structures of the glycopeptide sulfotransferase Teg12 in a complex with the teicoplanin aglycone." Biochemistry. 2010; 49(19): 4159-68. PubMed: 20361791
| Comments:Bick et al (2010) produced three crystal structures: Teg12-apo (PDB 3MGC), Teg12 binary complex with Teicoplanin Aglycone (PDB 3MG9) and Teg12 ternary complex with PAP and Teicoplanin Aglycone (PDB 3MGB).
According to Bick et al (2010), aa 204 serves as a hinge for the flexible GHL helix. In the ternary structure, GHL helix and a helix at aa 193-203 together form a single long helix. In the apo and binary structures, aa 204 acts as the hinge that allows the GHL helix to adopt additional conformations.
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References |
- Bick MJ, Banik JJ, Darst SA, Brady SF. "Crystal structures of the glycopeptide sulfotransferase Teg12 in a complex with the teicoplanin aglycone." Biochemistry. 2010; 49(19): 4159-68. PubMed: 20361791
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Comments |
Bick et al (2010) produced three crystal structures: Teg12-apo (PDB 3MGC), Teg12 binary complex with Teicoplanin Aglycone (PDB 3MG9) and Teg12 ternary complex with PAP and Teicoplanin Aglycone (PDB 3MGB).
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