DP00703: Teg12FASTA viewXML view

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



Functional narrative    

Molecular function inferred as sulfotransferase activity. (UniProt/InterPro)

Region 1: 37-43 Region 2: 127-137 Region 5: 204-204 Region 3: 204-215 Region 4: 216-250

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.


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:
  1. 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:
  1. 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).




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:
  1. 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:
  1. 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.




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:
  1. 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:
  1. 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.




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:
  1. 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:
  1. 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.




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:
  1. 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:
  1. 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.




References

  1. 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).


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