2bwc
From Proteopedia
(New page: 200px<br /> <applet load="2bwc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bwc, resolution 2.15Å" /> '''STRUCTURE OF ENDOGL...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2BWC is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Rhodothermus_marinus Rhodothermus marinus]] with SO4 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=2BWC OCA]]. | + | 2BWC is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Rhodothermus_marinus Rhodothermus marinus]] with SO4 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: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BWC OCA]]. |
==Reference== | ==Reference== | ||
Dimerisation and an increase in active site aromatic groups as adaptations to high temperatures: X-ray solution scattering and substrate-bound crystal structures of Rhodothermus marinus endoglucanase Cel12A., Crennell SJ, Cook D, Minns A, Svergun D, Andersen RL, Nordberg Karlsson E, J Mol Biol. 2006 Feb 10;356(1):57-71. Epub 2005 Nov 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16343530 16343530] | Dimerisation and an increase in active site aromatic groups as adaptations to high temperatures: X-ray solution scattering and substrate-bound crystal structures of Rhodothermus marinus endoglucanase Cel12A., Crennell SJ, Cook D, Minns A, Svergun D, Andersen RL, Nordberg Karlsson E, J Mol Biol. 2006 Feb 10;356(1):57-71. Epub 2005 Nov 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16343530 16343530] | ||
| + | [[Category: Cellulase]] | ||
[[Category: Rhodothermus marinus]] | [[Category: Rhodothermus marinus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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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 11:04:41 2007'' |
Revision as of 08:59, 30 October 2007
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STRUCTURE OF ENDOGLUCANASE 12A (CEL12A) FROM RHODOTHERMUS MARINUS IN COMPLEX WITH CELLOPENTAOSE (5 MINUTE SOAK)
Overview
Cellulose, a polysaccharide consisting of beta-1,4-linked glucose, is the, major component of plant cell walls and consequently one of the most, abundant biopolymers on earth. Carbohydrate polymers such as cellulose are, molecules with vast diversity in structure and function, and a, multiplicity of hydrolases operating in concert are required for, depolymerisation. The bacterium Rhodothermus marinus, isolated from, shallow water marine hot springs, produces a number of, carbohydrate-degrading enzymes including a family 12 cellulase Cel12A. The, structure of R.marinus Cel12A in the ligand-free form (at 1.54 angstroms), and structures of RmCel12A after crystals were soaked in cellopentaose for, two different lengths of time, have been determined. The shorter soaked, complex revealed the ... [(full description)]
About this Structure
2BWC is a [Single protein] structure of sequence from [Rhodothermus marinus] with SO4 and GOL as [ligands]. Active as [Cellulase], with EC number [3.2.1.4]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Dimerisation and an increase in active site aromatic groups as adaptations to high temperatures: X-ray solution scattering and substrate-bound crystal structures of Rhodothermus marinus endoglucanase Cel12A., Crennell SJ, Cook D, Minns A, Svergun D, Andersen RL, Nordberg Karlsson E, J Mol Biol. 2006 Feb 10;356(1):57-71. Epub 2005 Nov 22. PMID:16343530
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