2bw8
From Proteopedia
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- | [[Image:2bw8.gif|left|200px]]<br /><applet load="2bw8" size=" | + | [[Image:2bw8.gif|left|200px]]<br /><applet load="2bw8" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bw8, resolution 1.54Å" /> | caption="2bw8, resolution 1.54Å" /> | ||
'''NATIVE STRUCTURE OF ENDOGLUCANASE 12A (CEL12A) FROM RHODOTHERMUS MARINUS'''<br /> | '''NATIVE STRUCTURE OF ENDOGLUCANASE 12A (CEL12A) FROM RHODOTHERMUS MARINUS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
- | 2BW8 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 as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Known structural/functional Site: <scene name='pdbsite=SO4:So4 Binding Site For Chain A'>SO4</scene>. Full crystallographic information is available from [http:// | + | 2BW8 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 <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Known structural/functional Site: <scene name='pdbsite=SO4:So4+Binding+Site+For+Chain+A'>SO4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BW8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: glycoside hydrolase family 12]] | [[Category: glycoside hydrolase family 12]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:28:28 2008'' |
Revision as of 08:28, 3 February 2008
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NATIVE STRUCTURE OF ENDOGLUCANASE 12A (CEL12A) FROM RHODOTHERMUS MARINUS
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 conformation of unhydrolysed cellotetraose, while, cellopentaose had been degraded more completely during the longer soak., Comparison of these structures with those of mesophilic family 12, cellulases in complex with inhibitors and substrate revealed that RmCel12A, has a more extensive aromatic network in the active site cleft which, ejects products after hydrolysis. The substrate structure confirms that, during hydrolysis by family 12 cellulases glucose does not pass through a, (2,5)B conformation. Small-angle X-ray scattering analysis of RmCel12A, showed that the enzyme forms a loosely associated antiparallel dimer in, solution, which may target the enzyme to the antiparallel polymer strands, in cellulose.
About this Structure
2BW8 is a Single protein structure of sequence from Rhodothermus marinus with as ligand. Active as Cellulase, with EC number 3.2.1.4 Known structural/functional Site: . 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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