PDBsum entry: 2vy0

Hydrolase

PDB-id: 2vy0

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Description

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PROCHECK

Protein chains

264 a.a. *

Ligands

MPD ×2

MRD ×2

Metal ions

_CL ×3

_NA ×3

_CA ×2

Waters ×252

* Residue conservation analysis

Tools

Clefts Calculation

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PDB id:

2vy0

Name:

Hydrolase

Title:

The x-ray structure of endo-beta-1,3-glucanase from pyrococcus furiosus

Structure:

Endo-beta-1,3-glucanase. Chain: a, b. Fragment: residues 35-297. Engineered: yes

Source:

Pyrococcus furiosus. Organism_taxid: 2261. Expressed in: escherichia coli. Expression_system_taxid: 469008.

UniProt:

Chains A, B: O73951 (O73951_PYRFU)

Seq:

Struc:

Seq:

297 a.a.

Struc:

264 a.a.*

Key:

PfamA domain

Secondary structure

* PDB and UniProt seqs differ at 1 residue position (black cross)

Resolution:

2.16Å

R-factor:

0.193

R-free:

0.229

Authors:

A.Ilari,A.Fiorillo

Key ref:

A.Ilari et al. (2009). Crystal structure of a family 16 endoglucanase from the hyperthermophile Pyrococcus furiosus- structural basis of substrate recognition.. FEBS J, 276, 1048-1058. [PubMed id: 19154353] [DOI: 10.1111/j.1742-4658.2008.06848.x]

Date:

15-Jul-08

Release date:

24-Mar-09

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Clefts

Surface

Key reference

DOI no: 10.1111/j.1742-4658.2008.06848.x

FEBS J 276:1048-1058 (2009)

PubMed id: 19154353

Crystal structure of a family 16 endoglucanase from the hyperthermophile Pyrococcus furiosus- structural basis of substrate recognition.

A.Ilari, A.Fiorillo, S.Angelaccio, R.Florio, R.Chiaraluce, J.van der Oost, V.Consalvi.

ABSTRACT

Bacterial and archaeal endo-beta-1,3-glucanases that belong to glycoside hydrolase family 16 share a beta-jelly-roll fold, but differ significantly in sequence and in substrate specificity. The crystal structure of the laminarinase (EC 3.2.1.39) from the hyperthermophilic archaeon Pyrococcus furiosus (pfLamA) has been determined at 2.1 A resolution by molecular replacement. The pfLamA structure reveals a kink of six residues (72-77) at the entrance of the catalytic cleft. This peptide is absent in the endoglucanases from alkaliphilic Nocardiopsis sp. strain F96 and Bacillus macerans, two proteins displaying an overall fold similar to that of pfLamA, but with different substrate specificity. A deletion mutant of pfLamA, lacking residues 72-75, hydrolyses the mixed-linkage beta-1,3-1,4-glucan lichenan 10 times more efficiently than the wild-type protein, indicating the importance of the kink in substrate preference.