1oa7

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[[Image:1oa7.jpg|left|200px]]
[[Image:1oa7.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1oa7 |SIZE=350|CAPTION= <scene name='initialview01'>1oa7</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1oa7", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Cbi+Binding+Site+For+Chain+A'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CBI:CELLOBIOSE'>CBI</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1oa7| PDB=1oa7 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oa7 OCA], [http://www.ebi.ac.uk/pdbsum/1oa7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oa7 RCSB]</span>
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}}
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'''STRUCTURE OF MELANOCARPUS ALBOMYCES ENDOGLUCANASE IN COMPLEX WITH CELLOBIOSE'''
'''STRUCTURE OF MELANOCARPUS ALBOMYCES ENDOGLUCANASE IN COMPLEX WITH CELLOBIOSE'''
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[[Category: Hirvonen, M.]]
[[Category: Hirvonen, M.]]
[[Category: Papageorgiou, A C.]]
[[Category: Papageorgiou, A C.]]
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[[Category: cellulase]]
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[[Category: Cellulase]]
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[[Category: cellulose degradation]]
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[[Category: Cellulose degradation]]
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[[Category: glycoside hydrolase]]
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[[Category: Glycoside hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:35:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:42:12 2008''
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Revision as of 00:35, 3 May 2008

Template:STRUCTURE 1oa7

STRUCTURE OF MELANOCARPUS ALBOMYCES ENDOGLUCANASE IN COMPLEX WITH CELLOBIOSE


Overview

Cellulose, a polysaccharide of beta-1,4-linked D-glucosyl units, is the major component of plant cell walls and one of the most abundant biopolymers in nature. Cellulases (cellobiohydrolases and endoglucanases) are enzymes that catalyse the hydrolysis of cellulose to smaller oligosaccharides, a process of paramount importance in biotechnology. The thermophilic fungus Melanocarpus albomyces produces a 20 kDa endoglucanase known as 20K-cellulase that has been found particularly useful in the textile industry. The crystal structures of free 20K-cellulase and its complex with cellobiose have been determined at 2.0 A resolution. The enzyme, classified into the glycoside hydrolase family 45, exhibits the characteristic six-stranded beta-barrel found before in Humicola insolens endoglucanase V structure. However, the active site in the 20K-cellulase shows a closing of approximately 2.5-3.5A while a mobile loop identified previously in Humicola insolens endoglucanase V and implicated in the catalytic mechanism is well-defined in 20K-cellulase. In addition, the crystal structure of the cellobiose complex shows a shift in the cellobiose position at the substrate-binding cleft. It is therefore proposed that these alterations may reflect differences in the binding mechanism and catalytic action of the enzyme.

About this Structure

1OA7 is a Single protein structure of sequence from Melanocarpus albomyces. Full crystallographic information is available from OCA.

Reference

Crystal structure of a family 45 endoglucanase from Melanocarpus albomyces: mechanistic implications based on the free and cellobiose-bound forms., Hirvonen M, Papageorgiou AC, J Mol Biol. 2003 Jun 6;329(3):403-10. PMID:12767825 Page seeded by OCA on Sat May 3 03:35:13 2008

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