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1j8v

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{{STRUCTURE_1j8v| PDB=1j8v | SCENE= }}
{{STRUCTURE_1j8v| PDB=1j8v | SCENE= }}
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'''Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with 4'-nitrophenyl 3I-thiolaminaritrioside'''
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===Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with 4'-nitrophenyl 3I-thiolaminaritrioside===
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==Overview==
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Family 3 beta-D-glucan glucohydrolases are distributed widely in higher plants. The enzymes catalyze the hydrolytic removal of beta-D-glucosyl residues from nonreducing termini of a range of beta-D-glucans and beta-D-oligoglucosides. Their broad specificity can be explained by x-ray crystallographic data obtained from a barley beta-D-glucan glucohydrolase in complex with nonhydrolyzable S-glycoside substrate analogs and by molecular modeling of enzyme/substrate complexes. The glucosyl residue that occupies binding subsite -1 is locked tightly into a fixed position through extensive hydrogen bonding with six amino acid residues near the bottom of an active site pocket. In contrast, the glucosyl residue at subsite +1 is located between two Trp residues at the entrance of the pocket, where it is constrained less tightly. The relative flexibility of binding at subsite +1, coupled with the projection of the remainder of bound substrate away from the enzyme's surface, means that the overall active site can accommodate a range of substrates with variable spatial dispositions of adjacent beta-D-glucosyl residues. The broad specificity for glycosidic linkage type enables the enzyme to perform diverse functions during plant development.
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(as it appears on PubMed at http://www.pubmed.gov), where 12034895 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12034895}}
==About this Structure==
==About this Structure==
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[[Category: 2-domain fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:55:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:39:13 2008''

Revision as of 11:39, 1 July 2008

Image:1j8v.png

Template:STRUCTURE 1j8v

Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with 4'-nitrophenyl 3I-thiolaminaritrioside

Template:ABSTRACT PUBMED 12034895

About this Structure

1J8V is a Single protein structure of sequence from Hordeum vulgare. Full crystallographic information is available from OCA.

Reference

Structural basis for broad substrate specificity in higher plant beta-D-glucan glucohydrolases., Hrmova M, De Gori R, Smith BJ, Fairweather JK, Driguez H, Varghese JN, Fincher GB, Plant Cell. 2002 May;14(5):1033-52. PMID:12034895

Page seeded by OCA on Tue Jul 1 14:39:13 2008

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