1gpi
From Proteopedia
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'''CELLOBIOHYDROLASE CEL7D (CBH 58) FROM PHANEROCHAETE CHRYSOSPORIUM. CATALYTIC MODULE AT 1.32 ANG RESOLUTION''' | '''CELLOBIOHYDROLASE CEL7D (CBH 58) FROM PHANEROCHAETE CHRYSOSPORIUM. CATALYTIC MODULE AT 1.32 ANG RESOLUTION''' | ||
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[[Category: Munoz, I G.]] | [[Category: Munoz, I G.]] | ||
[[Category: Stahlberg, J.]] | [[Category: Stahlberg, J.]] | ||
| - | [[Category: | + | [[Category: Beta-glucanase]] |
| - | [[Category: | + | [[Category: Cellulase]] |
| - | [[Category: | + | [[Category: Cellulose degradation]] |
| - | [[Category: | + | [[Category: Enzyme]] |
| - | [[Category: | + | [[Category: Exoglucanase]] |
| - | [[Category: | + | [[Category: Extracellular]] |
| - | [[Category: | + | [[Category: Glycoprotein]] |
| - | [[Category: | + | [[Category: Glycosidase]] |
| - | [[Category: | + | [[Category: Reaction center]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:51:33 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 14:51, 2 May 2008
CELLOBIOHYDROLASE CEL7D (CBH 58) FROM PHANEROCHAETE CHRYSOSPORIUM. CATALYTIC MODULE AT 1.32 ANG RESOLUTION
Overview
Cellobiohydrolase 58 (Cel7D) is the major cellulase produced by the white-rot fungus Phanerochaete chrysosporium, constituting approximately 10 % of the total secreted protein in liquid culture on cellulose. The enzyme is classified into family 7 of the glycosyl hydrolases, together with cellobiohydrolase I (Cel7A) and endoglucanase I (Cel7B) from Trichoderma reesei. Like those enzymes, it catalyses cellulose hydrolysis with net retention of the anomeric carbon configuration.The structure of the catalytic module (431 residues) of Cel7D was determined at 3.0 A resolution using the structure of Cel7A from T. reesei as a search model in molecular replacement, and ultimately refined at 1.32 A resolution. The core structure is a beta-sandwich composed of two large and mainly antiparallel beta-sheets packed onto each other. A long cellulose-binding groove is formed by loops on one face of the sandwich. The catalytic residues are conserved and the mechanism is expected to be the same as for other family members. The Phanerochaete Cel7D binding site is more open than that of the T. reesei cellobiohydrolase, as a result of deletions and other changes in the loop regions, which may explain observed differences in catalytic properties. The binding site is not, however, as open as the groove of the corresponding endoglucanase. A tyrosine residue at the entrance of the tunnel may be part of an additional subsite not present in the T. reesei cellobiohydrolase.The Cel7D structure was used to model the products of the five other family 7 genes found in P. chrysosporium. The results suggest that at least two of these will have differences in specificity and possibly catalytic mechanism, thus offering some explanation for the presence of Cel7 isozymes in this species, which are differentially expressed in response to various growth conditions.
About this Structure
1GPI is a Single protein structure of sequence from Phanerochaete chrysosporium. Full crystallographic information is available from OCA.
Reference
Family 7 cellobiohydrolases from Phanerochaete chrysosporium: crystal structure of the catalytic module of Cel7D (CBH58) at 1.32 A resolution and homology models of the isozymes., Munoz IG, Ubhayasekera W, Henriksson H, Szabo I, Pettersson G, Johansson G, Mowbray SL, Stahlberg J, J Mol Biol. 2001 Dec 14;314(5):1097-111. PMID:11743726 Page seeded by OCA on Fri May 2 17:51:33 2008
