PDBsum entry 2zqz

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Oxidoreductase PDB id
Jmol PyMol
Protein chains
(+ 0 more) 307 a.a. *
SO4 ×12
Waters ×304
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: R-state structure of allosteric l-lactate dehydrogenase from lactobacillus casei
Structure: L-lactate dehydrogenase. Chain: a, b, c, d, e, f. Synonym: l-ldh. Engineered: yes
Source: Lactobacillus casei. Organism_taxid: 1582. Strain: iam 12473. Gene: ldh. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.50Å     R-factor:   0.212     R-free:   0.271
Authors: K.Arai,T.Ishimitsu,S.Fushinobu,H.Uchikoba,H.Matsuzawa, H.Taguchi
Key ref: K.Arai et al. (2010). Active and inactive state structures of unliganded Lactobacillus casei allosteric L-lactate dehydrogenase. Proteins, 78, 681-694. PubMed id: 19787773
22-Aug-08     Release date:   08-Sep-09    
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Protein chains
Pfam   ArchSchema ?
P00343  (LDH_LACCA) -  L-lactate dehydrogenase
326 a.a.
307 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - L-lactate dehydrogenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: (S)-lactate + NAD+ = pyruvate + NADH
+ NAD(+)
= pyruvate
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     oxidation-reduction process   3 terms 
  Biochemical function     catalytic activity     4 terms  


Proteins 78:681-694 (2010)
PubMed id: 19787773  
Active and inactive state structures of unliganded Lactobacillus casei allosteric L-lactate dehydrogenase.
K.Arai, T.Ishimitsu, S.Fushinobu, H.Uchikoba, H.Matsuzawa, H.Taguchi.
Lactobacillus casei L-lactate dehydrogenase (LCLDH) is activated through the homotropic and heterotropic activation effects of pyruvate and fructose 1,6-bisphosphate (FBP), respectively, and exhibits unusually high pH-dependence in the allosteric effects of these ligands. The active (R) and inactive (T) state structures of unliganded LCLDH were determined at 2.5 and 2.6 A resolution, respectively. In the catalytic site, the structural rearrangements are concerned mostly in switching of the orientation of Arg171 through the flexible intersubunit contact at the Q-axis subunit interface. The distorted orientation of Arg171 in the T state is stabilized by a unique intra-helix salt bridge between Arg171 and Glu178, which is in striking contrast to the multiple intersubunit salt bridges in Lactobacillus pentosus nonallosteric L-lactate dehydrogenase. In the backbone structure, major structural rearrangements of LCLDH are focused in two mobile regions of the catalytic domain. The two regions form an intersubunit linkage through contact at the P-axis subunit interface involving Arg185, replacement of which with Gln severely decreases the homotropic and hetertropic activation effects on the enzyme. These two regions form another intersubunit linkage in the Q-axis related dimer through the rigid NAD-binding domain, and thus constitute a pivotal frame of the intersubunit linkage for the allosteric motion, which is coupled with the concerted structural change of the four subunits in a tetramer, and of the binding sites for pyruvate and FBP. The unique intersubunit salt bridges, which are observed only in the R state structure, are likely involved in the pH-dependent allosteric equilibrium.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20852941 H.Xia, C.Wu, Q.Xu, J.Shi, F.Feng, K.Chen, Q.Yao, Y.Wang, and L.Wang (2011).
Molecular cloning and characterization of lactate dehydrogenase gene 1 in the silkworm, Bombyx mori.
  Mol Biol Rep, 38, 1853-1860.  
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