1j8v: Difference between revisions

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[[Image:1j8v.jpg|left|200px]]
{{Seed}}
[[Image:1j8v.png|left|200px]]


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{{STRUCTURE_1j8v|  PDB=1j8v  |  SCENE=  }}  
{{STRUCTURE_1j8v|  PDB=1j8v  |  SCENE=  }}  


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




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_12034895}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_12034895}}


==About this Structure==
==About this Structure==
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[[Category: 2-domain fold]]
[[Category: 2-domain fold]]
[[Category: Ligand-protein complex]]
[[Category: Ligand-protein complex]]
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