spacer
spacer

PDBsum entry 4adl

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Lyase PDB id
4adl
Jmol
Contents
Protein chains
459 a.a.
Ligands
LMR ×2
Waters ×1271
PDB id:
4adl
Name: Lyase
Title: Crystal structures of rv1098c in complex with malate
Structure: Fumarate hydratase class ii. Chain: a, b, c, d. Synonym: fumarasE C. Engineered: yes
Source: Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: h37rv. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: plyss.
Resolution:
2.20Å     R-factor:   0.155     R-free:   0.178
Authors: A.E.Mechaly,A.Haouz,I.Miras,P.Weber,W.Shepard,S.Cole,P.M.Alz M.Bellinzoni
Key ref: A.E.Mechaly et al. (2012). Conformational changes upon ligand binding in the essential class II fumarase Rv1098c from Mycobacterium tuberculosis. FEBS Lett, 586, 1606-1611. PubMed id: 22561013 DOI: 10.1016/j.febslet.2012.04.034
Date:
26-Dec-11     Release date:   25-Apr-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam  
P9WN93  (FUMC_MYCTU) -  Fumarate hydratase class II
Seq:
Struc:
474 a.a.
459 a.a.
Key:    Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.4.2.1.2  - Fumarate hydratase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Citric acid cycle
      Reaction: (S)-malate = fumarate + H2O
(S)-malate
Bound ligand (Het Group name = LMR)
corresponds exactly
= fumarate
+ H(2)O
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   6 terms 
  Biological process     growth   3 terms 
  Biochemical function     catalytic activity     3 terms  

 

 
    Added reference    
 
 
DOI no: 10.1016/j.febslet.2012.04.034 FEBS Lett 586:1606-1611 (2012)
PubMed id: 22561013  
 
 
Conformational changes upon ligand binding in the essential class II fumarase Rv1098c from Mycobacterium tuberculosis.
A.E.Mechaly, A.Haouz, I.Miras, N.Barilone, P.Weber, W.Shepard, P.M.Alzari, M.Bellinzoni.
 
  ABSTRACT  
 
No abstract given.