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PDBsum entry 2gqu

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protein ligands links
Oxidoreductase PDB id
2gqu
Jmol
Contents
Protein chain
266 a.a. *
Ligands
FAD
EPU
Waters ×407
* Residue conservation analysis
PDB id:
2gqu
Name: Oxidoreductase
Title: Crystal structure of udp-n-acetylenolpyruvylglucosamine reductase (murb) from thermus caldophilus
Structure: Udp-n-acetylenolpyruvylglucosamine reductase. Chain: a. Engineered: yes
Source: Thermus caldophilus. Organism_taxid: 272. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.60Å     R-factor:   0.172     R-free:   0.223
Authors: S.H.Eom,M.-K.Kim
Key ref:
M.K.Kim et al. (2007). Crystal structure of UDP-N-acetylenolpyruvylglucosamine reductase (MurB) from Thermus caldophilus. Proteins, 66, 751-754. PubMed id: 17120230 DOI: 10.1002/prot.21174
Date:
21-Apr-06     Release date:   19-Dec-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q5SJC8  (MURB_THET8) -  UDP-N-acetylenolpyruvoylglucosamine reductase
Seq:
Struc:
265 a.a.
266 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.3.1.98  - UDP-N-acetylmuramate dehydrogenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: UDP-N-acetyl-alpha-D-muramate + NADP+ = UDP-N-acetyl-3- O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH
UDP-N-acetyl-alpha-D-muramate
Bound ligand (Het Group name = EPU)
corresponds exactly
+ NADP(+)
= UDP-N-acetyl-3- O-(1-carboxyvinyl)-alpha-D-glucosamine
+ NADPH
      Cofactor: FAD
FAD
Bound ligand (Het Group name = FAD) corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     cell wall organization   6 terms 
  Biochemical function     catalytic activity     5 terms  

 

 
    reference    
 
 
DOI no: 10.1002/prot.21174 Proteins 66:751-754 (2007)
PubMed id: 17120230  
 
 
Crystal structure of UDP-N-acetylenolpyruvylglucosamine reductase (MurB) from Thermus caldophilus.
M.K.Kim, M.K.Cho, H.E.Song, D.Kim, B.H.Park, J.H.Lee, G.B.Kang, S.H.Kim, Y.J.Im, D.S.Lee, S.H.Eom.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. Crystal structure of Thermus caldophilus MurB. (A) T. caldophilus MurB structure with bound FAD cofactor (blue). (B) T. caldophilus MurB structure with bound FAD cofactor (blue) and EP-UDPGIcNAc substrate (red). (C) Superposition of the apo (gray) and substrate-complexed structures (blue). The arrow shows the conformational change in Domain 3 of the substrate-complexed structure when compared with the apo structure. (D) Secondary structure diagram for T. caldophilus MurB.
Figure 2.
Figure 2. Superimposition of the active sites of T. caldophilus MurB and Escherichia coli MurB. Residues for T. caldophilus MurB are shown in blue and the corresponding residues for E. coli MurB are shown in pink. Each black box indicates the active site residues involved in catalysis.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2007, 66, 751-754) copyright 2007.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18266853 H.Barreteau, A.Kovac, A.Boniface, M.Sova, S.Gobec, and D.Blanot (2008).
Cytoplasmic steps of peptidoglycan biosynthesis.
  FEMS Microbiol Rev, 32, 168-207.  
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