PDBsum entry: 1nof

Hydrolase

PDB-id: 1nof

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Protein chain

383 a.a. *

Ligands

ACT

Waters ×522

* Residue conservation analysis

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PDB id:

1nof

Name:

Hydrolase

Title:

The first crystallographic structure of a xylanase from glycosyl hydrolase family 5: implications for catalysis

Structure:

Xylanase. Chain: a. Engineered: yes

Source:

Erwinia chrysanthemi. Organism_taxid: 556. Gene: xyna. Expressed in: escherichia coli. Expression_system_taxid: 562.

UniProt:

Q46961 (Q46961_ERWCH)

Seq:

Struc:

Seq:

413 a.a.

Struc:

383 a.a.

Key:	PfamA domain
Secondary structure	CATH domain

Resolution:

1.42Å

R-factor:

0.108

R-free:

0.161

Authors:

S.B.Larson,J.Day,A.Mcpherson,A.P.Barba De La Rosa,N.T.Keen

Key ref:

S.B.Larson et al. (2003). First crystallographic structure of a xylanase from glycoside hydrolase family 5: implications for catalysis.. Biochemistry, 42, 8411-8422. [PubMed id: 12859186] [DOI: 10.1021/bi034144c]

Date:

16-Jan-03

Release date:

16-Sep-03

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Key reference

DOI no: 10.1021/bi034144c

Biochemistry 42:8411-8422 (2003)

PubMed id: 12859186

First crystallographic structure of a xylanase from glycoside hydrolase family 5: implications for catalysis.

S.B.Larson, J.Day, A.P.Barba de la Rosa, N.T.Keen, A.McPherson.

ABSTRACT

The room-temperature structure of xylanase (EC 3.2.1.8) from the bacterial plant pathogen Erwinia chrysanthemi expressed in Escherichia coli, a 45 kDa, 413-amino acid protein belonging to glycoside hydrolase family 5, has been determined by multiple isomorphous replacement and refined to a resolution of 1.42 A. This represents the first structure of a xylanase not belonging to either glycoside hydrolase family 10 or family 11. The enzyme is composed of two domains similar to most family 10 xylanases and the alpha-amylases. The catalytic domain (residues 46-315) has a (beta/alpha)(8)-barrel motif with a binding cleft along the C-terminal side of the beta-barrel. The catalytic residues, Glu165 and Glu253, determined by correspondence to other family 5 and family 10 glycoside hydrolases, lie inside this cleft on the C-terminal ends of beta-strands 4 and 7, respectively, with an O(epsilon)2...O(epsilon)1 distance of 4.22 A. The smaller domain (residues 31-43 and 323-413) has a beta(9)-barrel motif with five of the strands interfacing with alpha-helices 7 and 8 of the catalytic domain. The first 13 N-terminal residues form one beta-strand of this domain. Residues 44, 45, and 316-322 form the linkers between this domain and the catalytic domain.