PDBsum entry: 2wag

Hydrolase

PDB-id: 2wag

Contents

Description

Header details

Header records

References

PROCHECK

Protein chain

217 a.a. *

Ligands

15P ×5

SO4 ×5

GOL ×2

Metal ions

_MG

Waters ×372

* Residue conservation analysis

Tools

Clefts Calculation

PDB id:

2wag

Name:

Hydrolase

Title:

The structure of a family 25 glycosyl hydrolase from bacillus anthracis.

Structure:

Lysozyme, putative. Chain: a. Fragment: catalytic domain, residues 37-245. Synonym: family gh25 lysozyme. Engineered: yes

Source:

Bacillus anthracis. Organism_taxid: 198094. Strain: ames. Expressed in: escherichia coli. Expression_system_taxid: 469008.

UniProt:

Q81YN8 (Q81YN8_BACAN)

Seq:

245 a.a.

Struc:

217 a.a.*

Key:

PfamA domain

Secondary structure

* PDB and UniProt seqs differ at 9 residue positions (black crosses)

Resolution:

1.40Å

R-factor:

0.188

R-free:

0.212

Authors:

C.Martinez-Fleites,J.E.Korczynska,M.Cope,J.P.Turkenburg, E.J.Taylor

Key ref:

C.Martinez-Fleites et al. (2009). The crystal structure of a family GH25 lysozyme from Bacillus anthracis implies a neighboring-group catalytic mechanism with retention of anomeric configuration.. Carbohydr Res, 344, 1753-1757. [PubMed id: 19595298] [DOI: 10.1016/j.carres.2009.06.001]

Date:

06-Feb-09

Release date:

23-Jun-09

Quick_links

Procheck

Clefts

Surface

Key reference

DOI no: 10.1016/j.carres.2009.06.001

Carbohydr Res 344:1753-1757 (2009)

PubMed id: 19595298

The crystal structure of a family GH25 lysozyme from Bacillus anthracis implies a neighboring-group catalytic mechanism with retention of anomeric configuration.

C.Martinez-Fleites, J.E.Korczynska, G.J.Davies, M.J.Cope, J.P.Turkenburg, E.J.Taylor.

ABSTRACT

Lysozymes are found in many of the sequence-based families of glycoside hydrolases (www.cazy.org) where they show considerable structural and mechanistic diversity. Lysozymes from glycoside hydrolase family GH25 adopt a (alpha/beta)(5)(beta)(3)-barrel-like fold with a proposal in the literature that these enzymes act with inversion of anomeric configuration; the lack of a suitable substrate, however, means that no group has successfully demonstrated the configuration of the product. Here we report the 3-D structure of the GH25 enzyme from Bacillus anthracis at 1.4A resolution. We show that the active center is extremely similar to those from glycoside hydrolase families GH18, GH20, GH56, GH84, and GH85 implying that, in the absence of evidence to the contrary, GH25 enzymes also act with net retention of anomeric configuration using the neighboring-group catalytic mechanism that is common to this 'super-family' of enzymes.