1z3w: Difference between revisions

Revision as of 18:21, 27 July 2008

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File:1z3w.png

Template:STRUCTURE 1z3w

Structure of Phanerochaete chrysosporium cellobiohydrolase Cel7D (CBH58) in complex with cellobioimidazoleStructure of Phanerochaete chrysosporium cellobiohydrolase Cel7D (CBH58) in complex with cellobioimidazole

Template:ABSTRACT PUBMED 15819888

About this StructureAbout this Structure

1Z3W is a Single protein structure of sequence from Phanerochaete chrysosporium. Full crystallographic information is available from OCA.

ReferenceReference

Structures of Phanerochaete chrysosporium Cel7D in complex with product and inhibitors., Ubhayasekera W, Munoz IG, Vasella A, Stahlberg J, Mowbray SL, FEBS J. 2005 Apr;272(8):1952-64. PMID:15819888

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

The catalytic module of Cel7D from Phanerochaete chrysosporium as a chiral selector: structural studies of its complex with the beta blocker (R)-propranolol., Munoz IG, Mowbray SL, Stahlberg J, Acta Crystallogr D Biol Crystallogr. 2003 Apr;59(Pt 4):637-43. Epub 2003, Mar 25. PMID:12657782

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-'''Structure of Phanerochaete chrysosporium cellobiohydrolase Cel7D (CBH58) in complex with cellobioimidazole'''
+===Structure of Phanerochaete chrysosporium cellobiohydrolase Cel7D (CBH58) in complex with cellobioimidazole===
-==Overview==
+<!--
-The cellobiohydrolase Pc_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 glycoside hydrolases and, like other family members, catalyses cellulose hydrolysis with net retention of the anomeric carbon configuration. Previous work described the apo structure of the enzyme. Here we investigate the binding of the product, cellobiose, and several inhibitors, i.e. lactose, cellobioimidazole, Tris/HCl, calcium and a thio-linked substrate analogue, methyl 4-S-beta-cellobiosyl-4-thio-beta-cellobioside (GG-S-GG). The three disaccharides bind in the glucosyl-binding subsites +1 and +2, close to the exit of the cellulose-binding tunnel/cleft. Pc_Cel7D binds to lactose more strongly than cellobiose, while the opposite is true for the homologous Trichoderma reesei cellobiohydrolase Tr_Cel7A. Although both sugars bind Pc_Cel7D in a similar fashion, the different preferences can be explained by varying interactions with nearby loops. Cellobioimidazole is bound at a slightly different position, displaced approximately 2 A toward the catalytic centre. Thus the Pc_Cel7D complexes provide evidence for two binding modes of the reducing-end cellobiosyl moiety; this conclusion is confirmed by comparison with other available structures. The combined results suggest that hydrolysis of the glycosyl-enzyme intermediate may not require the prior release of the cellobiose product from the enzyme. Further, the structure obtained in the presence of both GG-S-GG and cellobiose revealed electron density for Tris at the catalytic centre. Inhibition experiments confirm that both Tris and calcium are effective inhibitors at the conditions used for crystallization.
+The line below this paragraph, {{ABSTRACT_PUBMED_15819888}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15819888 is the PubMed ID number.
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 ==About this Structure==
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 ==Reference==
 Structures of Phanerochaete chrysosporium Cel7D in complex with product and inhibitors., Ubhayasekera W, Munoz IG, Vasella A, Stahlberg J, Mowbray SL, FEBS J. 2005 Apr;272(8):1952-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15819888 15819888]
+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:[http://www.ncbi.nlm.nih.gov/pubmed/11743726 11743726]
+The catalytic module of Cel7D from Phanerochaete chrysosporium as a chiral selector: structural studies of its complex with the beta blocker (R)-propranolol., Munoz IG, Mowbray SL, Stahlberg J, Acta Crystallogr D Biol Crystallogr. 2003 Apr;59(Pt 4):637-43. Epub 2003, Mar 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12657782 12657782]
 [[Category: Cellulose 1,4-beta-cellobiosidase]]
 [[Category: Phanerochaete chrysosporium]]
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 [[Category: Vasella, A.]]
 [[Category: Beta sandwich]]
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