This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1byh
From Proteopedia
(New page: 200px<br /><applet load="1byh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1byh, resolution 2.8Å" /> '''MOLECULAR AND ACTIVE-...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1byh.gif|left|200px]]<br /><applet load="1byh" size=" | + | [[Image:1byh.gif|left|200px]]<br /><applet load="1byh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1byh, resolution 2.8Å" /> | caption="1byh, resolution 2.8Å" /> | ||
'''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== | ||
| - | The three-dimensional structure of the hybrid Bacillus | + | 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== | ||
| - | 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:// | + | 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== | ||
| Line 20: | Line 20: | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''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
|
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
Page seeded by OCA on Thu Feb 21 12:00:32 2008
Categories: Licheninase | Single protein | Synthetic construct | Heinemann, U. | Keitel, T. | CA | NBU | Hydrolase
