1j8v
From Proteopedia
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| - | [[Image:1j8v.jpg|left|200px]] | + | [[Image:1j8v.jpg|left|200px]] |
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| - | '''Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with 4'-nitrophenyl 3I-thiolaminaritrioside''' | + | {{Structure |
| + | |PDB= 1j8v |SIZE=350|CAPTION= <scene name='initialview01'>1j8v</scene>, resolution 2.40Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=LAM:4'-NITROPHENYL-S-(BETA-D-GLUCOPYRANOSYL)-(1-3)-(3-THIO-BETA-D-GLUCOPYRANOSYL)-(1-3)-BETA-D-GLUCOPYRANOSIDE'>LAM</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Glucan_1,3-beta-glucosidase Glucan 1,3-beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.58 3.2.1.58] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with 4'-nitrophenyl 3I-thiolaminaritrioside''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1J8V is a [ | + | 1J8V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J8V OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12034895 12034895] |
[[Category: Glucan 1,3-beta-glucosidase]] | [[Category: Glucan 1,3-beta-glucosidase]] | ||
[[Category: Hordeum vulgare]] | [[Category: Hordeum vulgare]] | ||
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[[Category: ligand-protein complex]] | [[Category: ligand-protein complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:00:09 2008'' |
Revision as of 10:00, 20 March 2008
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| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Glucan 1,3-beta-glucosidase, with EC number 3.2.1.58 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with 4'-nitrophenyl 3I-thiolaminaritrioside
Overview
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.
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
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