1j8v
From Proteopedia
(New page: 200px<br /><applet load="1j8v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j8v, resolution 2.40Å" /> '''Crystal structure of...) |
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| - | [[Image:1j8v.jpg|left|200px]]<br /><applet load="1j8v" size=" | + | [[Image:1j8v.jpg|left|200px]]<br /><applet load="1j8v" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1j8v, resolution 2.40Å" /> | caption="1j8v, resolution 2.40Å" /> | ||
'''Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with 4'-nitrophenyl 3I-thiolaminaritrioside'''<br /> | '''Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with 4'-nitrophenyl 3I-thiolaminaritrioside'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Family 3 beta-D-glucan glucohydrolases are distributed widely in higher | + | 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== | ==About this Structure== | ||
| - | 1J8V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare] with LAM as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1J8V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare] with <scene name='pdbligand=LAM:'>LAM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J8V OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Driguez, H.]] | [[Category: Driguez, H.]] | ||
| - | [[Category: Fairweather, J | + | [[Category: Fairweather, J K.]] |
| - | [[Category: Fincher, G | + | [[Category: Fincher, G B.]] |
| - | [[Category: Gori, R | + | [[Category: Gori, R De.]] |
[[Category: Hrmova, M.]] | [[Category: Hrmova, M.]] | ||
| - | [[Category: Smith, B | + | [[Category: Smith, B J.]] |
| - | [[Category: Varghese, J | + | [[Category: Varghese, J N.]] |
[[Category: LAM]] | [[Category: LAM]] | ||
[[Category: 2-domain fold]] | [[Category: 2-domain fold]] | ||
[[Category: ligand-protein complex]] | [[Category: ligand-protein complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:20:10 2008'' |
Revision as of 11:20, 21 February 2008
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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 with as ligand. Active as Glucan 1,3-beta-glucosidase, with EC number 3.2.1.58 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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