1gbg
From Proteopedia
(New page: 200px<br /><applet load="1gbg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gbg, resolution 1.8Å" /> '''BACILLUS LICHENIFORMI...) |
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| - | [[Image:1gbg.gif|left|200px]]<br /><applet load="1gbg" size=" | + | [[Image:1gbg.gif|left|200px]]<br /><applet load="1gbg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1gbg, resolution 1.8Å" /> | caption="1gbg, resolution 1.8Å" /> | ||
'''BACILLUS LICHENIFORMIS BETA-GLUCANASE'''<br /> | '''BACILLUS LICHENIFORMIS BETA-GLUCANASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the 1,3-1,4-beta-D-glucan 4-glucanohydrolase from | + | The crystal structure of the 1,3-1,4-beta-D-glucan 4-glucanohydrolase from Bacillus licheniformis is solved at a resolution of 1.8 A and refined to R = 16.5%. The protein has a similar beta-sandwich structure as the homologous enzyme from Bacillus macerans and the hybrid H(A16-M). This demonstrates that the jellyroll fold of these proteins is remarkably rigid and only weakly influenced by crystal contacts. The crystal structure permits to extend mechanistic considerations derived for the B. licheniformis enzyme to the entire class of bacterial 1,3-1,4-beta-D-glucan 4-glucanohydrolases. |
==About this Structure== | ==About this Structure== | ||
| - | 1GBG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1GBG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1GBG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase (glucanase)]] | [[Category: hydrolase (glucanase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:16 2008'' |
Revision as of 10:48, 21 February 2008
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BACILLUS LICHENIFORMIS BETA-GLUCANASE
Overview
The crystal structure of the 1,3-1,4-beta-D-glucan 4-glucanohydrolase from Bacillus licheniformis is solved at a resolution of 1.8 A and refined to R = 16.5%. The protein has a similar beta-sandwich structure as the homologous enzyme from Bacillus macerans and the hybrid H(A16-M). This demonstrates that the jellyroll fold of these proteins is remarkably rigid and only weakly influenced by crystal contacts. The crystal structure permits to extend mechanistic considerations derived for the B. licheniformis enzyme to the entire class of bacterial 1,3-1,4-beta-D-glucan 4-glucanohydrolases.
About this Structure
1GBG is a Single protein structure of sequence from Bacillus licheniformis with as ligand. Active as Licheninase, with EC number 3.2.1.73 Full crystallographic information is available from OCA.
Reference
Crystal structure of Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase at 1.8 A resolution., Hahn M, Pons J, Planas A, Querol E, Heinemann U, FEBS Lett. 1995 Oct 30;374(2):221-4. PMID:7589539
Page seeded by OCA on Thu Feb 21 12:48:16 2008
