1byh: Difference between revisions

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{{STRUCTURE_1byh|  PDB=1byh  |  SCENE=  }}  
{{STRUCTURE_1byh|  PDB=1byh  |  SCENE=  }}  


'''MOLECULAR AND ACTIVE-SITE STRUCTURE OF A BACILLUS (1-3,1-4)-BETA-GLUCANASE'''
===MOLECULAR AND ACTIVE-SITE STRUCTURE OF A BACILLUS (1-3,1-4)-BETA-GLUCANASE===




==Overview==
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The three-dimensional structure of the hybrid Bacillus 1,3-1,4-beta-glucanase (beta-glucanase; 1,3-1,4-beta-D-glucan 4-glucanohydrolase, lichenase, EC 3.2.1.73) designated H(A16-M) was determined by x-ray crystallography at a resolution of 2.0 A and refined to an R value of 16.4% using stereochemical restraints. The protein molecule consists mainly of two seven-stranded antiparallel beta-pleated sheets arranged atop each other to form a compact, sandwich-like structure. A channel crossing one side of the protein molecule accommodates an inhibitor, 3,4-epoxybutyl beta-D-cellobioside, which binds covalently to the side chain of Glu-105, as seen in a crystal structure analysis at 2.8-A resolution of the protein-inhibitor complex (R = 16.8%). That Glu-105 may be indispensible for enzyme catalysis by H(A16-M) is suggested by site-directed mutagenesis of this residue, which inevitably leads to an inactive enzyme.
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{{ABSTRACT_PUBMED_8099449}}


==About this Structure==
==About this Structure==
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[[Category: Keitel, T.]]
[[Category: Keitel, T.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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Revision as of 16:57, 30 June 2008

File:1byh.png

Template:STRUCTURE 1byh

MOLECULAR AND ACTIVE-SITE STRUCTURE OF A BACILLUS (1-3,1-4)-BETA-GLUCANASE

Template:ABSTRACT PUBMED 8099449

About this Structure

1BYH is a Single protein structure of sequence from Synthetic construct. Full crystallographic information is available from OCA.

Reference

Molecular and active-site structure of a Bacillus 1,3-1,4-beta-glucanase., Keitel T, Simon O, Borriss R, Heinemann U, Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5287-91. PMID:8099449

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