PDBsum entry 3lez

Hydrolase

PDB id

3lez

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Contents

			Protein chain

					260 a.a. *

			Ligands

					EPE

			Metals

					_CA ×8


					_CL

			Waters ×515

* Residue conservation analysis

PDB id:

3lez

Links

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

Resolution:

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

Date:

15-Jan-10

Release date:

02-Feb-10

PROCHECK

	Headers

	References

Protein chain

Q8EMP8 (Q8EMP8_OCEIH) - Beta-lactamase from Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831)

Seq: Struc:					304 a.a. 260 a.a.

Key:

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.3.5.2.6 - beta-lactamase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Pathway:

Penicillin Biosynthesis and Metabolism

Reaction:

a beta-lactam + H2O = a substituted beta-amino acid

Cofactor:

Zn(2+)

	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.

ABSTRACT

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.

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.