PDBsum entry 4xhc

Hydrolase

PDB id: 4xhc

Contents

Protein chains

513 a.a.

Ligands

RAM ×2

SO4 ×4

Waters ×45

PDB id:

4xhc

Name:

Hydrolase

Title:

Rhamnosidase from klebsiella oxytoca with rhamnose bound

Structure:

Alpha-l-rhamnosidase. Chain: a, b. Engineered: yes. Other_details: the n terminal tag was not cleaved prior to crystallisation

Source:

Klebsiella oxytoca. Organism_taxid: 571. Gene: kox_19945. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.70Å R-factor: 0.183 R-free: 0.202

Authors:

E.O.O'Neill,C.E.M.Stevenson,M.J.Patterson,M.Rejzek,A.Chauvin, D.M.Lawson,R.A.Field

Key ref:

E.C.O'Neill et al. (2015). Crystal structure of a novel two domain GH78 family α-rhamnosidase from Klebsiella oxytoca with rhamnose bound. Proteins, 83, 1742-1749. PubMed id: 25846411 DOI: 10.1002/prot.24807

Date:

05-Jan-15 Release date: 15-Apr-15

Protein chains

A0A0J9X262  (A0A0J9X262_KLEOX) -  alpha-L-rhamnosidase from Klebsiella oxytoca

Seq: 523 a.a.

Struc: 513 a.a.

Enzyme reactions

• Enzyme class: E.C.3.2.1.40 - alpha-L-rhamnosidase.
• Reaction: Hydrolysis of terminal non-reducing alpha-L-rhamnoase residues in alpha-L-rhamnosides.

DOI no: 10.1002/prot.24807

Proteins 83:1742-1749 (2015)

PubMed id: 25846411

Crystal structure of a novel two domain GH78 family α-rhamnosidase from Klebsiella oxytoca with rhamnose bound.

E.C.O'Neill, C.E.Stevenson, M.J.Paterson, M.Rejzek, A.L.Chauvin, D.M.Lawson, R.A.Field.

ABSTRACT

The crystal structure of the GH78 family α-rhamnosidase from Klebsiella oxytoca (KoRha) has been determined at 2.7 Å resolution with rhamnose bound in the active site of the catalytic domain. Curiously, the putative catalytic acid, Asp 222, is preceded by an unusual non-proline cis-peptide bond which helps to project the carboxyl group into the active centre. This KoRha homodimeric structure is significantly smaller than those of the other previously determined GH78 structures. Nevertheless, the enzyme displays α-rhamnosidase activity when assayed in vitro, suggesting that the additional structural domains found in the related enzymes are dispensible for function. Proteins 2015; 83:1742-1749. © 2015 The Authors. Proteins: Structure, Function, and Bioinformatics Published by Wiley Periodicals, Inc.