1qox

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[[Image:1qox.gif|left|200px]]<br /><applet load="1qox" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1qox.gif|left|200px]]
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caption="1qox, resolution 2.7&Aring;" />
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'''BETA-GLUCOSIDASE FROM BACILLUS CIRCULANS SP. ALKALOPHILUS'''<br />
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{{Structure
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|PDB= 1qox |SIZE=350|CAPTION= <scene name='initialview01'>1qox</scene>, resolution 2.7&Aring;
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|SITE= <scene name='pdbsite=CAA:Active+Site+(Chain+A)'>CAA</scene>, <scene name='pdbsite=CAB:Active+Site+(Chain+B)'>CAB</scene>, <scene name='pdbsite=CAC:Active+Site+(Chain+C)'>CAC</scene>, <scene name='pdbsite=CAD:Active+Site+(Chain+D)'>CAD</scene>, <scene name='pdbsite=CAE:Active+Site+(Chain+E)'>CAE</scene>, <scene name='pdbsite=CAF:Active+Site+(Chain+F)'>CAF</scene>, <scene name='pdbsite=CAG:Active+Site+(Chain+G)'>CAG</scene>, <scene name='pdbsite=CAH:Active+Site+(Chain+H)'>CAH</scene>, <scene name='pdbsite=CAI:Active+Site+(Chain+I)'>CAI</scene>, <scene name='pdbsite=CAJ:Active+Site+(Chain+J)'>CAJ</scene>, <scene name='pdbsite=CAK:Active+Site+(Chain+K)'>CAK</scene>, <scene name='pdbsite=CAL:Active+Site+(Chain+L)'>CAL</scene>, <scene name='pdbsite=CAM:Active+Site+(Chain+M)'>CAM</scene>, <scene name='pdbsite=CAN:Active+Site+(Chain+N)'>CAN</scene>, <scene name='pdbsite=CAO:Active+Site+(Chain+O)'>CAO</scene> and <scene name='pdbsite=CAP:Active+Site+(Chain+P)'>CAP</scene>
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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=
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}}
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'''BETA-GLUCOSIDASE FROM BACILLUS CIRCULANS SP. ALKALOPHILUS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1QOX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans]. 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] Known structural/functional Sites: <scene name='pdbsite=CAA:Active+Site+(Chain+A)'>CAA</scene>, <scene name='pdbsite=CAB:Active+Site+(Chain+B)'>CAB</scene>, <scene name='pdbsite=CAC:Active+Site+(Chain+C)'>CAC</scene>, <scene name='pdbsite=CAD:Active+Site+(Chain+D)'>CAD</scene>, <scene name='pdbsite=CAE:Active+Site+(Chain+E)'>CAE</scene>, <scene name='pdbsite=CAF:Active+Site+(Chain+F)'>CAF</scene>, <scene name='pdbsite=CAG:Active+Site+(Chain+G)'>CAG</scene>, <scene name='pdbsite=CAH:Active+Site+(Chain+H)'>CAH</scene>, <scene name='pdbsite=CAI:Active+Site+(Chain+I)'>CAI</scene>, <scene name='pdbsite=CAJ:Active+Site+(Chain+J)'>CAJ</scene>, <scene name='pdbsite=CAK:Active+Site+(Chain+K)'>CAK</scene>, <scene name='pdbsite=CAL:Active+Site+(Chain+L)'>CAL</scene>, <scene name='pdbsite=CAM:Active+Site+(Chain+M)'>CAM</scene>, <scene name='pdbsite=CAN:Active+Site+(Chain+N)'>CAN</scene>, <scene name='pdbsite=CAO:Active+Site+(Chain+O)'>CAO</scene> and <scene name='pdbsite=CAP:Active+Site+(Chain+P)'>CAP</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOX OCA].
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1QOX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOX OCA].
==Reference==
==Reference==
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The crystal structure of beta-glucosidase from Bacillus circulans sp. alkalophilus: ability to form long polymeric assemblies., Hakulinen N, Paavilainen S, Korpela T, Rouvinen J, J Struct Biol. 2000 Feb;129(1):69-79. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10675298 10675298]
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The crystal structure of beta-glucosidase from Bacillus circulans sp. alkalophilus: ability to form long polymeric assemblies., Hakulinen N, Paavilainen S, Korpela T, Rouvinen J, J Struct Biol. 2000 Feb;129(1):69-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10675298 10675298]
[[Category: Bacillus circulans]]
[[Category: Bacillus circulans]]
[[Category: Beta-glucosidase]]
[[Category: Beta-glucosidase]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:42:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:40:39 2008''

Revision as of 11:40, 20 March 2008


PDB ID 1qox

Drag the structure with the mouse to rotate
, resolution 2.7Å
Sites: , , , , , , , , , , , , , , and
Activity: Beta-glucosidase, with EC number 3.2.1.21
Coordinates: save as pdb, mmCIF, xml



BETA-GLUCOSIDASE FROM BACILLUS CIRCULANS SP. ALKALOPHILUS


Overview

Family 1 of glycosyl hydrolases is a large and biologically important group of enzymes. A new three-dimensional structure of this family, beta-glucosidase from Bacillus circulans sp. alkalophilus is reported here. This is the first structure of beta-glucosidase from an alkaliphilic organism. The model was determined by the molecular replacement method and refined to a resolution of 2.7 A. The quaternary structure of B. circulans sp. alkalophilus beta-glucosidase is an octamer and subunits of the octamer show a similar (beta/alpha)(8) barrel fold to that previously reported for other family 1 enzymes. The crystal structure suggested that Cys169 in the active site is substituted. The Cys169 is located near the putative acid/base catalyst Glu166 and it may contribute to the high pH optimum of the enzyme. The crystal structure also revealed that the asymmetric unit contains two octamers which have a clear binding interaction with each other. The ability of the octamers to link with each other suggested that beta-glucosidase from Bacillus circulans sp. alkalophilus is able to form long polymeric assemblies, at least in the crystalline state.

About this Structure

1QOX is a Single protein structure of sequence from Bacillus circulans. Full crystallographic information is available from OCA.

Reference

The crystal structure of beta-glucosidase from Bacillus circulans sp. alkalophilus: ability to form long polymeric assemblies., Hakulinen N, Paavilainen S, Korpela T, Rouvinen J, J Struct Biol. 2000 Feb;129(1):69-79. PMID:10675298

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