1hf6
From Proteopedia
(New page: 200px<br /> <applet load="1hf6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hf6, resolution 1.15Å" /> '''ENDOGLUCANASE CEL5A...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1HF6 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_agaradhaerens Bacillus agaradhaerens]] with SO4, CT3, ACY and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HF6 OCA]]. | + | 1HF6 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_agaradhaerens Bacillus agaradhaerens]] with SO4, CT3, ACY and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Cellulase Cellulase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4]]. Structure known Active Site: ACI. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HF6 OCA]]. |
==Reference== | ==Reference== | ||
Direct experimental observation of the hydrogen-bonding network of a glycosidase along its reaction coordinate revealed by atomic resolution analyses of endoglucanase Cel5A., Varrot A, Davies GJ, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):447-52. Epub 2003, Feb 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12595701 12595701] | Direct experimental observation of the hydrogen-bonding network of a glycosidase along its reaction coordinate revealed by atomic resolution analyses of endoglucanase Cel5A., Varrot A, Davies GJ, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):447-52. Epub 2003, Feb 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12595701 12595701] | ||
[[Category: Bacillus agaradhaerens]] | [[Category: Bacillus agaradhaerens]] | ||
| + | [[Category: Cellulase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Davies, G.J.]] | [[Category: Davies, G.J.]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:49:16 2007'' |
Revision as of 11:44, 30 October 2007
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ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHAERENS IN THE ORTHORHOMBIC CRYSTAL FORM IN COMPLEX WITH CELLOTRIOSE
Overview
Non-covalent interactions between protein and ligand at the active centre, of glycosidases play an enormous role in catalysis. Dissection of these, hydrogen-bonding networks is not merely important for an understanding of, enzymatic catalysis, but is also increasingly relevant for the design of, transition-state mimics, whose tautomeric state, hydrogen-bonding, interactions and protonation contribute to tight binding. Here, atomic, resolution ( approximately 1 A) analysis of a series of complexes of the, 34 kDa catalytic core domain of the Bacillus agaradhaerens endoglucanase, Cel5A is presented. Cel5A is a 'retaining' endoglucanase which performs, catalysis via the formation and subsequent breakdown of a covalent, glycosyl-enzyme intermediate via oxocarbenium-ion-like transition states., ... [(full description)]
About this Structure
1HF6 is a [Single protein] structure of sequence from [Bacillus agaradhaerens] with SO4, CT3, ACY and GOL as [ligands]. Active as [Cellulase], with EC number [3.2.1.4]. Structure known Active Site: ACI. Full crystallographic information is available from [OCA].
Reference
Direct experimental observation of the hydrogen-bonding network of a glycosidase along its reaction coordinate revealed by atomic resolution analyses of endoglucanase Cel5A., Varrot A, Davies GJ, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):447-52. Epub 2003, Feb 21. PMID:12595701
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