PoplarV1, Main, Exploration, bibRecord, 004295

Crystal structures of a poplar xyloglucan endotransglycosylase reveal details of transglycosylation acceptor binding.

Identifieur interne : 004295 ( Main/Exploration ); précédent : 004294; suivant : 004296

Crystal structures of a poplar xyloglucan endotransglycosylase reveal details of transglycosylation acceptor binding.

Auteurs : Patrik Johansson [Suède] ; Harry Brumer ; Martin J. Baumann ; Asa M. Kallas ; Hongbin Henriksson ; Stuart E. Denman ; Tuula T. Teeri ; T Alwyn Jones

Source :

The Plant cell [ 1040-4651 ] ; 2004.

RBID : pubmed:15020748

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Binding Sites (MeSH), Carbohydrate Sequence (MeSH), Crystallography, X-Ray (MeSH), Glucans (chemistry), Glycosylation (MeSH), Glycosyltransferases (chemistry), Glycosyltransferases (genetics), Glycosyltransferases (metabolism), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Oligosaccharides (chemistry), Pichia (genetics), Populus (enzymology), Populus (genetics), Protein Conformation (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Sequence Homology, Amino Acid (MeSH), Xylans (chemistry).
MESH :
- chemical , chemistry : Glucans, Glycosyltransferases, Oligosaccharides, Recombinant Proteins, Xylans.
- chemical , genetics : Glycosyltransferases, Recombinant Proteins.
- chemical , metabolism : Glycosyltransferases, Recombinant Proteins.
- enzymology : Populus.
- genetics : Pichia, Populus.
- Amino Acid Sequence, Binding Sites, Carbohydrate Sequence, Crystallography, X-Ray, Glycosylation, Models, Molecular, Molecular Sequence Data, Protein Conformation, Sequence Homology, Amino Acid.

Abstract

Xyloglucan endotransglycosylases (XETs) cleave and religate xyloglucan polymers in plant cell walls via a transglycosylation mechanism. Thus, XET is a key enzyme in all plant processes that require cell wall remodeling. To provide a basis for detailed structure-function studies, the crystal structure of Populus tremula x tremuloides XET16A (PttXET16A), heterologously expressed in Pichia pastoris, has been determined at 1.8-A resolution. Even though the overall structure of PttXET16A is a curved beta-sandwich similar to other enzymes in the glycoside hydrolase family GH16, parts of its substrate binding cleft are more reminiscent of the distantly related family GH7. In addition, XET has a C-terminal extension that packs against the conserved core, providing an additional beta-strand and a short alpha-helix. The structure of XET in complex with a xyloglucan nonasaccharide, XLLG, reveals a very favorable acceptor binding site, which is a necessary but not sufficient prerequisite for transglycosylation. Biochemical data imply that the enzyme requires sugar residues in both acceptor and donor sites to properly orient the glycosidic bond relative to the catalytic residues.

DOI: 10.1105/tpc.020065
PubMed: 15020748
PubMed Central: PMC412862

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 004320
to stream Main, to step Curation: 004320

Le document en format XML

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<term>Données de séquences moléculaires (MeSH)</term>
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<term>Glycosyltransferase (composition chimique)</term>
<term>Glycosyltransferase (génétique)</term>
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<term>Sites de fixation (MeSH)</term>
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<front><div type="abstract" xml:lang="en">Xyloglucan endotransglycosylases (XETs) cleave and religate xyloglucan polymers in plant cell walls via a transglycosylation mechanism. Thus, XET is a key enzyme in all plant processes that require cell wall remodeling. To provide a basis for detailed structure-function studies, the crystal structure of Populus tremula x tremuloides XET16A (PttXET16A), heterologously expressed in Pichia pastoris, has been determined at 1.8-A resolution. Even though the overall structure of PttXET16A is a curved beta-sandwich similar to other enzymes in the glycoside hydrolase family GH16, parts of its substrate binding cleft are more reminiscent of the distantly related family GH7. In addition, XET has a C-terminal extension that packs against the conserved core, providing an additional beta-strand and a short alpha-helix. The structure of XET in complex with a xyloglucan nonasaccharide, XLLG, reveals a very favorable acceptor binding site, which is a necessary but not sufficient prerequisite for transglycosylation. Biochemical data imply that the enzyme requires sugar residues in both acceptor and donor sites to properly orient the glycosidic bond relative to the catalytic residues.</div>
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<Abstract><AbstractText>Xyloglucan endotransglycosylases (XETs) cleave and religate xyloglucan polymers in plant cell walls via a transglycosylation mechanism. Thus, XET is a key enzyme in all plant processes that require cell wall remodeling. To provide a basis for detailed structure-function studies, the crystal structure of Populus tremula x tremuloides XET16A (PttXET16A), heterologously expressed in Pichia pastoris, has been determined at 1.8-A resolution. Even though the overall structure of PttXET16A is a curved beta-sandwich similar to other enzymes in the glycoside hydrolase family GH16, parts of its substrate binding cleft are more reminiscent of the distantly related family GH7. In addition, XET has a C-terminal extension that packs against the conserved core, providing an additional beta-strand and a short alpha-helix. The structure of XET in complex with a xyloglucan nonasaccharide, XLLG, reveals a very favorable acceptor binding site, which is a necessary but not sufficient prerequisite for transglycosylation. Biochemical data imply that the enzyme requires sugar residues in both acceptor and donor sites to properly orient the glycosidic bond relative to the catalytic residues.</AbstractText>
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Crystal structures of a poplar xyloglucan endotransglycosylase reveal details of transglycosylation acceptor binding.

Crystal structures of a poplar xyloglucan endotransglycosylase reveal details of transglycosylation acceptor binding.

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