1byh

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(New page: 200px<br /><applet load="1byh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1byh, resolution 2.8&Aring;" /> '''MOLECULAR AND ACTIVE-...)
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caption="1byh, resolution 2.8&Aring;" />
'''MOLECULAR AND ACTIVE-SITE STRUCTURE OF A BACILLUS (1-3,1-4)-BETA-GLUCANASE'''<br />
'''MOLECULAR AND ACTIVE-SITE STRUCTURE OF A BACILLUS (1-3,1-4)-BETA-GLUCANASE'''<br />
==Overview==
==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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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.
==About this Structure==
==About this Structure==
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1BYH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct] with CA and NBU as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Licheninase Licheninase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.73 3.2.1.73] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BYH OCA].
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1BYH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=NBU:'>NBU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Licheninase Licheninase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.73 3.2.1.73] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYH OCA].
==Reference==
==Reference==
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:01:36 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:32 2008''

Revision as of 10:00, 21 February 2008

Image:1byh.gif

1byh, resolution 2.8Å

Drag the structure with the mouse to rotate

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

Overview

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.

About this Structure

1BYH is a Single protein structure of sequence from Synthetic construct with and as ligands. Active as Licheninase, with EC number 3.2.1.73 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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