1vff

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[[Image:1vff.gif|left|200px]]<br /><applet load="1vff" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1vff.gif|left|200px]]
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caption="1vff, resolution 2.50&Aring;" />
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'''beta-glycosidase from Pyrococcus horikoshii'''<br />
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{{Structure
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|PDB= 1vff |SIZE=350|CAPTION= <scene name='initialview01'>1vff</scene>, resolution 2.50&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21]
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|GENE= PH0366 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=53953 Pyrococcus horikoshii])
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}}
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'''beta-glycosidase from Pyrococcus horikoshii'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1VFF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Active as [http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VFF OCA].
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1VFF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VFF OCA].
==Reference==
==Reference==
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X-ray structure of a membrane-bound beta-glycosidase from the hyperthermophilic archaeon Pyrococcus horikoshii., Akiba T, Nishio M, Matsui I, Harata K, Proteins. 2004 Nov 1;57(2):422-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15340929 15340929]
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X-ray structure of a membrane-bound beta-glycosidase from the hyperthermophilic archaeon Pyrococcus horikoshii., Akiba T, Nishio M, Matsui I, Harata K, Proteins. 2004 Nov 1;57(2):422-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15340929 15340929]
[[Category: Beta-glucosidase]]
[[Category: Beta-glucosidase]]
[[Category: Pyrococcus horikoshii]]
[[Category: Pyrococcus horikoshii]]
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[[Category: Matsui, I.]]
[[Category: Matsui, I.]]
[[Category: Nishio, M.]]
[[Category: Nishio, M.]]
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[[Category: alkylglucosides]]
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[[Category: alkylglucoside]]
[[Category: glycosyl hydrolase]]
[[Category: glycosyl hydrolase]]
[[Category: membrane-bound enzyme]]
[[Category: membrane-bound enzyme]]
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[[Category: tim barrel]]
[[Category: tim barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:34:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:44:49 2008''

Revision as of 12:44, 20 March 2008


PDB ID 1vff

Drag the structure with the mouse to rotate
, resolution 2.50Å
Gene: PH0366 (Pyrococcus horikoshii)
Activity: Beta-glucosidase, with EC number 3.2.1.21
Coordinates: save as pdb, mmCIF, xml



beta-glycosidase from Pyrococcus horikoshii


Overview

The beta-glycosidase of the hyperthermophilic Archaeon Pyrococcus horikoshii is a membrane-bound enzyme with the preferred substrate of alkyl-beta-glycosides. In this study, the unusual structural features that confer the extreme thermostability and substrate preferences of this enzyme were investigated by X-ray crystallography and docking simulation. The enzyme was crystallized in the presence of a neutral surfactant, and the crystal structure was solved by the molecular replacement method and refined at 2.5 A. The main-chain fold of the enzyme belongs to the (betaalpha)8 barrel structure common to the Family 1 glycosyl hydrolases. The active site is located at the center of the C-termini of the barrel beta-strands. The deep pocket of the active site accepts one sugar unit, and a hydrophobic channel extending radially from there binds the nonsugar moiety of the substrate. The docking simulation for oligosaccharides and alkylglucosides indicated that alkylglucosides with a long aliphatic chain are easily accommodated in the hydrophobic channel. This sparingly soluble enzyme has a cluster of hydrophobic residues on its surface, situated at the distal end of the active site channel and surrounded by a large patch of positively charged residues. We propose that this hydrophobic region can be inserted into the membrane while the surrounding positively charged residues make favorable contacts with phosphate groups on the inner surface of the membrane. The enzyme could thus adhere to the membrane in the proximity of its glycolipid substrate.

About this Structure

1VFF is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.

Reference

X-ray structure of a membrane-bound beta-glycosidase from the hyperthermophilic archaeon Pyrococcus horikoshii., Akiba T, Nishio M, Matsui I, Harata K, Proteins. 2004 Nov 1;57(2):422-31. PMID:15340929

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