spacer
spacer

PDBsum entry 3okc

Go to PDB code: 
protein ligands links
Transferase PDB id
3okc

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chain
378 a.a. *
Ligands
GDP
Waters ×140
* Residue conservation analysis
PDB id:
3okc
Name: Transferase
Title: Crystal structure of corynebacterium glutamicum pimb' bound to gdp (orthorhombic crystal form)
Structure: Gdp-mannose-dependent alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase. Chain: a. Synonym: guanosine diphosphomannose-phosphatidyl-inositol alpha- mannosyltransferase, phosphatidylinositol alpha-mannosyltransferase, pi alpha-mannosyltransferase, alpha-mannosyltransferase, alpha-mant, alpha-d-mannose-alpha-(1-6)-phosphatidylmyo-inositol- mannosyltransferase. Engineered: yes
Source: Corynebacterium glutamicum. Brevibacterium flavum. Organism_taxid: 1718. Gene: cg2400, cgl2186, ncgl2106, pimb. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.40Å     R-factor:   0.192     R-free:   0.236
Authors: S.M.Batt,T.Jabeen,G.S.Besra,K.Futterer
Key ref: S.M.Batt et al. (2010). Acceptor substrate discrimination in phosphatidyl-myo-inositol mannoside synthesis: structural and mutational analysis of mannosyltransferase Corynebacterium glutamicum PimB'. J Biol Chem, 285, 37741-37752. PubMed id: 20843801
Date:
24-Aug-10     Release date:   15-Sep-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q8NNK8  (PIMB_CORGL) -  GDP-mannose-dependent monoacylated alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)
Seq:
Struc:
381 a.a.
378 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.4.1.346  - phosphatidyl-myo-inositol dimannoside synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. a 1,2-diacyl-sn-glycero-3-phospho-[alpha-D-mannopyranosyl-(1<->6)-D- myo-inositol] + GDP-alpha-D-mannose = a 2,6-O-bis(alpha-D- mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + GDP + H+
2. a 1,2-diacyl-sn-glycero-3-phospho-[alpha-D-6-acyl-mannopyranosyl- (1<->6)-D-myo-inositol] + GDP-alpha-D-mannose = a 2-O-(alpha-D-mannosyl)- 6-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + GDP + H+
1,2-diacyl-sn-glycero-3-phospho-[alpha-D-mannopyranosyl-(1<->6)-D- myo-inositol]
+ GDP-alpha-D-mannose
= 2,6-O-bis(alpha-D- mannopyranosyl)-1-phosphatidyl-1D-myo-inositol
+
GDP
Bound ligand (Het Group name = GDP)
corresponds exactly
+ H(+)
1,2-diacyl-sn-glycero-3-phospho-[alpha-D-6-acyl-mannopyranosyl- (1<->6)-D-myo-inositol]
+ GDP-alpha-D-mannose
= 2-O-(alpha-D-mannosyl)- 6-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
+
GDP
Bound ligand (Het Group name = GDP)
corresponds exactly
+ H(+)
      Cofactor: Mg(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
J Biol Chem 285:37741-37752 (2010)
PubMed id: 20843801  
 
 
Acceptor substrate discrimination in phosphatidyl-myo-inositol mannoside synthesis: structural and mutational analysis of mannosyltransferase Corynebacterium glutamicum PimB'.
S.M.Batt, T.Jabeen, A.K.Mishra, N.Veerapen, K.Krumbach, L.Eggeling, G.S.Besra, K.Fütterer.
 
  ABSTRACT  
 
No abstract given.

 

 

spacer

spacer