1oa7
From Proteopedia
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| - | [[Image:1oa7.jpg|left|200px]] | + | [[Image:1oa7.jpg|left|200px]] |
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| - | '''STRUCTURE OF MELANOCARPUS ALBOMYCES ENDOGLUCANASE IN COMPLEX WITH CELLOBIOSE''' | + | {{Structure |
| + | |PDB= 1oa7 |SIZE=350|CAPTION= <scene name='initialview01'>1oa7</scene>, resolution 2.0Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Cbi+Binding+Site+For+Chain+A'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=CBI:CELLOBIOSE'>CBI</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF MELANOCARPUS ALBOMYCES ENDOGLUCANASE IN COMPLEX WITH CELLOBIOSE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OA7 is a [ | + | 1OA7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Melanocarpus_albomyces Melanocarpus albomyces]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OA7 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12767825 12767825] |
[[Category: Cellulase]] | [[Category: Cellulase]] | ||
[[Category: Melanocarpus albomyces]] | [[Category: Melanocarpus albomyces]] | ||
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[[Category: cellulase]] | [[Category: cellulase]] | ||
[[Category: cellulose degradation]] | [[Category: cellulose degradation]] | ||
| - | [[Category: glycoside | + | [[Category: glycoside hydrolase]] |
| - | ''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 13:08:00 2008'' |
Revision as of 11:08, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Cellulase, with EC number 3.2.1.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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