PDBsum entry 1iyx

Go to PDB code: 
protein ligands metals Protein-protein interface(s) links
Lyase PDB id
Protein chains
431 a.a. *
SO4 ×2
GOL ×6
_MG ×2
Waters ×162
* Residue conservation analysis
PDB id:
Name: Lyase
Title: Crystal structure of enolase from enterococcus hirae
Structure: Enolase. Chain: a, b. Ec:
Source: Enterococcus hirae. Organism_taxid: 1354
Biol. unit: Dimer (from PQS)
2.80Å     R-factor:   0.175     R-free:   0.239
Authors: T.Hosaka,T.Meguro,I.Yamato,Y.Shirakihara
Key ref: T.Hosaka et al. (2003). Crystal structure of Enterococcus hirae enolase at 2.8 A resolution. J Biochem, 133, 817-823. PubMed id: 12869539
12-Sep-02     Release date:   29-Jul-03    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q8GR70  (ENO_ENTHR) -  Enolase
432 a.a.
431 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Phosphopyruvate hydratase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2-phospho-D-glycerate = phosphoenolpyruvate + H2O
Bound ligand (Het Group name = GOL)
matches with 54.55% similarity
= phosphoenolpyruvate
+ H(2)O
      Cofactor: Mg(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   4 terms 
  Biological process     glycolysis   1 term 
  Biochemical function     lyase activity     4 terms  


    Added reference    
J Biochem 133:817-823 (2003)
PubMed id: 12869539  
Crystal structure of Enterococcus hirae enolase at 2.8 A resolution.
T.Hosaka, T.Meguro, I.Yamato, Y.Shirakihara.
We report the crystal structure of an enolase from Enterococcus hirae, which is the first report of a structure determination among gram-positive bacteria. We isolated the enolase gene and determined the base sequence. The amino acid sequence deduced from the DNA sequence suggests that this enolase is composed of 431 amino acids. The amino acid sequence is very similar to those of enolases from eukaryotic and prokaryotic organisms, being 65% and 50% identical to enolases from Escherichia coli and yeast, respectively. The enolase prepared from E. hirae lysate yielded crystals containing one dimer per asymmetric unit. X-ray diffraction patterns were obtained at 2.8 A resolution on a SPring-8 synchrotron radiation source. Crystals belong to space group I4 with unit cell dimensions of a = b = 153.5 A, c = 90.7 A. The E. hirae, yeast, E. coli and lobster enolase structures are very similar. The E. hirae enolase takes an "Open" conformation. The regions in the structure that differ most from other enolases are loops L4 (132-140) and L3 (244-265). Considering the positions of these loops relative to the active site, they seem to have no direct involvement in function. Our findings show that the three dimensional structure of an important enzyme in the glycolytic pathway is evolutionarily conserved among eukaryotes and prokaryotes, including gram-positive bacteria.

Literature references that cite this PDB file's key reference

  PubMed id Reference
  19255486 J.Wang, Y.F.Zhou, L.F.Li, and X.D.Su (2009).
Crystallization and preliminary X-ray analysis of human liver alpha-enolase.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 288-290.  
19622860 T.Hosaka, K.Murayama, M.Kato-Murayama, A.Urushibata, R.Akasaka, T.Terada, M.Shirouzu, S.Kuramitsu, and S.Yokoyama (2009).
Structure of the putative thioesterase protein TTHA1846 from Thermus thermophilus HB8 complexed with coenzyme A and a zinc ion.
  Acta Crystallogr D Biol Crystallogr, 65, 767-776.
PDB code: 2cye
18560153 H.J.Kang, S.K.Jung, S.J.Kim, and S.J.Chung (2008).
Structure of human alpha-enolase (hENO1), a multifunctional glycolytic enzyme.
  Acta Crystallogr D Biol Crystallogr, 64, 651-657.
PDB code: 3b97
  18997349 H.Yamamoto, and N.Kunishima (2008).
Purification, crystallization and preliminary crystallographic study of the putative enolase MJ0232 from the hyperthermophilic archaeon Methanococcus jannaschii.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 1087-1090.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.