PDBsum entry 3lez

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Hydrolase PDB id
Protein chain
260 a.a. *
_CA ×8
Waters ×515
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Crystal structure of a halotolerant bacterial beta-lactamase
Structure: Beta-lactamase. Chain: a. Fragment: mature beta-lactamase. Engineered: yes
Source: Oceanobacillus iheyensis. Organism_taxid: 182710. Gene: ob2793, oih-1. Expressed in: escherichia coli. Expression_system_taxid: 562
1.25Å     R-factor:   0.155     R-free:   0.174
Authors: C.A.Smith,S.B.Vakulenko
Key ref: M.Toth et al. (2010). An antibiotic-resistance enzyme from a deep-sea bacterium. J Am Chem Soc, 132, 816-823. PubMed id: 20000704
15-Jan-10     Release date:   02-Feb-10    
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Protein chain
Pfam   ArchSchema ?
Q8EMP8  (Q8EMP8_OCEIH) -  Beta-lactamase
304 a.a.
260 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Beta-lactamase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Penicillin Biosynthesis and Metabolism
      Reaction: A beta-lactam + H2O = a substituted beta-amino acid
      Cofactor: Zinc
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     response to antibiotic   2 terms 
  Biochemical function     beta-lactamase activity     1 term  


J Am Chem Soc 132:816-823 (2010)
PubMed id: 20000704  
An antibiotic-resistance enzyme from a deep-sea bacterium.
M.Toth, C.Smith, H.Frase, S.Mobashery, S.Vakulenko.
We describe herein a highly proficient class A beta-lactamase OIH-1 from the bacterium Oceanobacillus iheyensis, whose habitat is the sediment at a depth of 1050 m in the Pacific Ocean. The OIH-1 structure was solved by molecular replacement and refined at 1.25 A resolution. OIH-1 has evolved to be an extremely halotolerant beta-lactamase capable of hydrolyzing its substrates in the presence of NaCl at saturating concentration. Not only is this the most highly halotolerant bacterial enzyme structure known to date, it is also the highest resolution halophilic protein structure yet determined. Evolution of OIH-1 in the salinity of the ocean has resulted in a molecular surface that is coated with acidic residues, a marked difference from beta-lactamases of terrestrial sources. OIH-1 is the first example of an antibiotic-resistance enzyme that has evolved in the depths of the ocean in isolation from clinical selection and gives us an extraordinary glimpse into protein evolution under extreme conditions. It represents evidence for the existence of a reservoir of antibiotic-resistance enzymes in nature among microbial populations from deep oceanic sources.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21468894 B.Zheng, S.Tan, J.Gao, H.Han, J.Liu, G.Lu, D.Liu, Y.Yi, B.Zhu, and G.F.Gao (2011).
An unexpected similarity between antibiotic-resistant NDM-1 and beta-lactamase II from Erythrobacter litoralis.
  Protein Cell, 2, 250-258.  
21057784 P.Singh, C.Raghukumar, P.Verma, and Y.Shouche (2011).
Fungal community analysis in the deep-sea sediments of the Central Indian Basin by culture-independent approach.
  Microb Ecol, 61, 507-517.  
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