PDBsum entry: 2vh9

Hydrolase

PDB-id: 2vh9

Contents

Description

Header details

Header records

References

PROCHECK

Protein chains

266 a.a. *

Ligands

GOL ×2

BGC-BGC-BGC-BGC-XYS-GAL-XYS-GAL-XYS ×2

Metal ions

_ZN ×2

Waters ×515

* Residue conservation analysis

Tools

Clefts Calculation

PDB id:

2vh9

Name:

Hydrolase

Title:

Crystal structure of nxg1-deltayniig in complex with xllg, a xyloglucan derived oligosaccharide

Structure:

Cellulase. Chain: a, b. Synonym: xyloglucan hydrolase. Engineered: yes

Source:

Tropaeolum majus. Nasturtium. Organism_taxid: 4020. Tissue: seedling. Expressed in: pichia pastoris. Expression_system_taxid: 4922.

UniProt:

Chains A, B: Q07524 (Q07524_TROMA)

Seq:

Struc:

Seq:

295 a.a.

Struc:

266 a.a.

Key:

PfamA domain

Secondary structure

Enzyme class:

E.C.3.2.1.4   [IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Reaction:

Endohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Resolution:

2.1Å

R-factor:

0.151

R-free:

0.203

Authors:

M.Czjzek,P.Mark,M.J.Baumann,J.M.Eklof,G.Michel,H.Brumer

Key ref:

P.Mark et al. (2008). Analysis of nasturtium TmNXG1 complexes by crystallography and molecular dynamics provides detailed insight into substrate recognition by family GH16 xyloglucan endo-transglycosylases and endo-hydrolases.. Proteins, 75, 820-836. [PubMed id: 19004021] [DOI: 10.1002/prot.22291]

Date:

20-Nov-07

Release date:

25-Nov-08

Related entries:

2uwa crystal structure of the nasturtium seedling xyloglucanase isoform nxg1
2uwb crystal structure of the nasturtium seedling mutant xyloglucanase isoform nxg1-delta-yniig
2uwc crystal structure of nasturtium xyloglucan hydrolase isoform nxg2

Quick_links

Procheck

Clefts

Surface

Key reference

DOI no: 10.1002/prot.22291

Proteins 75:820-836 (2008)

PubMed id: 19004021

Analysis of nasturtium TmNXG1 complexes by crystallography and molecular dynamics provides detailed insight into substrate recognition by family GH16 xyloglucan endo-transglycosylases and endo-hydrolases.

P.Mark, M.J.Baumann, J.M.Eklöf, F.Gullfot, G.Michel, A.M.Kallas, T.T.Teeri, H.Brumer, M.Czjzek.

ABSTRACT

Reorganization and degradation of the wall crosslinking and seed storage polysaccharide xyloglucan by glycoside hydrolase family 16 (GH16) endo-transglycosylases and hydrolases are crucial to the growth of the majority of land plants, affecting processes as diverse as germination, morphogenesis, and fruit ripening. A high-resolution, three-dimensional structure of a nasturtium (Tropaeolum majus) endo-xyloglucanase loop mutant, TmNXG1-DeltaYNIIG, with an oligosaccharide product bound in the negative active-site subsites, has been solved by X-ray crystallography. Comparison of this novel complex to that of the strict xyloglucan endo-transglycosylase PttXET16-34 from hybrid aspen (Populus tremula x tremuloides), previously solved with a xylogluco-oligosaccharide bound in the positive subsites, highlighted key protein structures that affect the disparate catalytic activities displayed by these closely related enzymes. Combination of these "partial" active-site complexes through molecular dynamics simulations in water allowed modeling of wild-type TmNXG1, TmNXG1-DeltaYNIIG, and wild-type PttXET16-34 in complex with a xyloglucan octadecasaccharide spanning the entire catalytic cleft. A comprehensive analysis of these full-length complexes underscored the importance of various loops lining the active site. Subtle differences leading to a tighter hydrogen bonding pattern on the negative (glycosyl donor) binding subsites, together with loop flexibility on the positive (glycosyl acceptor) binding subsites appear to favor hydrolysis over transglycosylation in GH16 xyloglucan-active enzymes. Proteins 2009. (c) 2008 Wiley-Liss, Inc.