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PDBsum entry 3uww

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protein ligands metals Protein-protein interface(s) links
Isomerase PDB id
3uww
Jmol
Contents
Protein chains
254 a.a.
Ligands
DTT
3PG ×2
Metals
_NA
Waters ×211
PDB id:
3uww
Name: Isomerase
Title: Crystal structure of staphylococcus aureus triosephosphate i complexed with 3-phosphoglyceric acid
Structure: Triosephosphate isomerase. Chain: a, b. Synonym: tim, triose-phosphate isomerase. Engineered: yes
Source: Staphylococcus aureus. Organism_taxid: 282458. Strain: mrsa252. Gene: sar0830, tpi, tpia. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.25Å     R-factor:   0.209     R-free:   0.248
Authors: S.Mukherjee,A.Roychowdhury,D.Dutta,A.K.Das
Key ref: S.Mukherjee et al. (2012). Crystal structures of triosephosphate isomerase from methicillin resistant Staphylococcus aureus MRSA252 provide structural insights into novel modes of ligand binding and unique conformations of catalytic loop. Biochimie, 94, 2532-2544. PubMed id: 22813930 DOI: 10.1016/j.biochi.2012.07.001
Date:
03-Dec-11     Release date:   17-Oct-12    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q6GIL6  (TPIS_STAAR) -  Triosephosphate isomerase
Seq:
Struc:
253 a.a.
254 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.5.3.1.1  - Triose-phosphate isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: D-glyceraldehyde 3-phosphate = glycerone phosphate
D-glyceraldehyde 3-phosphate
Bound ligand (Het Group name = 3PG)
matches with 90.91% similarity
= glycerone phosphate
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     metabolic process   4 terms 
  Biochemical function     catalytic activity     3 terms  

 

 
    Added reference    
 
 
DOI no: 10.1016/j.biochi.2012.07.001 Biochimie 94:2532-2544 (2012)
PubMed id: 22813930  
 
 
Crystal structures of triosephosphate isomerase from methicillin resistant Staphylococcus aureus MRSA252 provide structural insights into novel modes of ligand binding and unique conformations of catalytic loop.
S.Mukherjee, A.Roychowdhury, D.Dutta, A.K.Das.
 
  ABSTRACT  
 
Staphylococcus aureus is one of the most dreaded pathogens worldwide and emergence of notorious antibiotic resistant strains have further exacerbated the present scenario. The glycolytic enzyme, triosephosphate isomerase (TIM) is one of the cell envelope proteins of the coccus and is involved in biofilm formation. It also plays an instrumental role in adherence and invasion of the bacteria into the host cell. To structurally characterize this important enzyme and analyze it's interaction with different inhibitors, substrate and transition state analogues, the present article describes several crystal structures of SaTIM alone and in complex with different ligands: glycerol-3-phosphate (G3P), glycerol-2-phosphate (G2P), 3-phosphoglyceric acid (3PG) and 2-phosphoglyceric acid (2PG). Unique conformations of the catalytic loop 6 (L6) has been observed in the different complexes. It is found to be in "almost closed" conformation in both subunits of the structure complexed to G3P. However L6 adopts the open conformation in presence of G2P and 2PG. The preference of the conformation of the catalytic loop can be correlated with the position of the phosphate group in the ligand. Novel modes of binding have been observed for G2P and 3PG for the very first time. The triose moiety is oriented away from the catalytic residues and occupies an entirely different position in some subunits. A completely new binding site for phosphate has also been identified in the complex with 2PG which differs substantially from the conventional phosphate binding site of the ligand in the crystal structures of TIM determined so far.