PDBsum entry 3zyt

Hydrolase

PDB id: 3zyt

Contents

Protein chain

372 a.a.

Ligands

EMC ×3

Waters ×147

PDB id:

3zyt

Name:

Hydrolase

Title:

Structure determination of esta from arthrobacter nitroguajacolicus rue61a

Structure:

Esterase a. Chain: a. Synonym: esta. Engineered: yes

Source:

Arthrobacter nitroguajacolicus. Organism_taxid: 211146. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: plyss.

Resolution:

2.45Å R-factor: 0.181 R-free: 0.216

Authors:

U.G.Wagner,S.Fetzner

Key ref:

U.G.Wagner et al. (2014). Crystal structure analysis of EstA from Arthrobacter sp. Rue61a--an insight into catalytic promiscuity. Febs Lett, 588, 1154-1160. PubMed id: 24613918 DOI: 10.1016/j.febslet.2014.02.045

Date:

25-Aug-11 Release date: 19-Sep-12

Protein chain

K4DIE4  (K4DIE4_PAENT) -  Esterase a from Paenarthrobacter nitroguajacolicus

Seq: 372 a.a.

Struc: 372 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.febslet.2014.02.045

Febs Lett 588:1154-1160 (2014)

PubMed id: 24613918

Crystal structure analysis of EstA from Arthrobacter sp. Rue61a--an insight into catalytic promiscuity.

U.G.Wagner, F.DiMaio, S.Kolkenbrock, S.Fetzner.

ABSTRACT

In this article we analyze the reasons for catalytic promiscuity of a type VIII esterase with β-lactamase fold and the ability to cleave β-lactams. We compared the structure of this enzyme to those of an esterase of the same type without any lactamase ability, an esterase with moderate lactamase ability, and a class C β-lactamase with similar fold. Our results show that for these enzymes, the difference in the substrate specificity is sterically driven.