PDBsum entry 5aoc

Hydrolase

PDB id: 5aoc

Contents

Protein chain

277 a.a.

Ligands

LEA

PG4 ×2

EDO ×7

PEG ×3

Metals

_CL

Waters ×214

PDB id:

5aoc

Name:

Hydrolase

Title:

The structure of a novel thermophilic esterase from the planctomycetes species, thermogutta terrifontis, est2-valerate bound

Structure:

Esterase. Chain: a. Engineered: yes

Source:

Thermogutta terrifontis. Organism_taxid: 1331910. Strain: r1. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.79Å R-factor: 0.188 R-free: 0.241

Authors:

C.Sayer,Z.Szabo,M.N.Isupov,C.Ingham,J.A.Littlechild

Key ref:

C.Sayer et al. (2015). The Structure of a Novel Thermophilic Esterase from the Planctomycetes Species, Thermogutta terrifontis Reveals an Open Active Site Due to a Minimal 'Cap' Domain. Front Microbiol, 6, 1294. PubMed id: 26635762 DOI: 10.3389/fmicb.2015.01294

Date:

10-Sep-15 Release date: 09-Dec-15

Protein chain

A0A0X1KHD1  (A0A0X1KHD1_9BACT) -  Esterase from Thermogutta terrifontis

Seq: 286 a.a.

Struc: 277 a.a.

Enzyme reactions

• Enzyme class: E.C.3.1.1.1 - carboxylesterase.
• Reaction: a carboxylic ester + H2O = an alcohol + a carboxylate + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.3389/fmicb.2015.01294

Front Microbiol 6:1294 (2015)

PubMed id: 26635762

The Structure of a Novel Thermophilic Esterase from the Planctomycetes Species, Thermogutta terrifontis Reveals an Open Active Site Due to a Minimal 'Cap' Domain.

C.Sayer, Z.Szabo, M.N.Isupov, C.Ingham, J.A.Littlechild.

ABSTRACT

A carboxyl esterase (TtEst2) has been identified in a novel thermophilic bacterium, Thermogutta terrifontis from the phylum Planctomycetes and has been cloned and over-expressed in Escherichia coli. The enzyme has been characterized biochemically and shown to have activity toward small p-nitrophenyl (pNP) carboxylic esters with optimal activity for pNP-acetate. The enzyme shows moderate thermostability retaining 75% activity after incubation for 30 min at 70°C. The crystal structures have been determined for the native TtEst2 and its complexes with the carboxylic acid products propionate, butyrate, and valerate. TtEst2 differs from most enzymes of the α/β-hydrolase family 3 as it lacks the majority of the 'cap' domain and its active site cavity is exposed to the solvent. The bound ligands have allowed the identification of the carboxyl pocket in the enzyme active site. Comparison of TtEst2 with structurally related enzymes has given insight into how differences in their substrate preference can be rationalized based upon the properties of their active site pockets.