1h0b
From Proteopedia
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| - | [[Image:1h0b.gif|left|200px]]<br /><applet load="1h0b" size=" | + | [[Image:1h0b.gif|left|200px]]<br /><applet load="1h0b" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1h0b, resolution 1.80Å" /> | caption="1h0b, resolution 1.80Å" /> | ||
'''ENDOGLUCANASE CEL12A FROM RHODOTHERMUS MARINUS'''<br /> | '''ENDOGLUCANASE CEL12A FROM RHODOTHERMUS MARINUS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1H0B 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 EPE 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=HE1:Epe Binding Site For Chain B'>HE1</scene>. Full crystallographic information is available from [http:// | + | 1H0B 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=EPE:'>EPE</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=HE1:Epe+Binding+Site+For+Chain+B'>HE1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H0B OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:44:43 2008'' |
Revision as of 07:44, 3 February 2008
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ENDOGLUCANASE CEL12A FROM RHODOTHERMUS MARINUS
Overview
Cellulose is one of the most abundant polysaccharides in nature and, microorganisms have developed a comprehensive system for enzymatic, breakdown of this ubiquitous carbon source, a subject of much interest in, the biotechnology industry. Rhodothermus marinus produces a, hyperthermostable cellulase, with a temperature optimum of more than 90, degrees C, the structure of which is presented here to 1.8 A resolution., The enzyme has been classified into glycoside hydrolase family 12; this is, the first structure of a thermophilic member of this family to have been, solved. The beta-jelly roll fold observed has identical topology to those, of the two mesophilic members of the family whose structures have been, elucidated previously. A Hepes buffer molecule bound in the active site, may have triggered a conformational change to an active configuration as, the two catalytic residues Glu124 and Glu207, together with dependent, residues, are observed in a conformation similar to that seen in the, structure of Streptomyces lividans CelB2 complexed with an inhibitor. The, structural similarity between this cellulase and the mesophilic enzymes, serves to highlight features that may be responsible for its, thermostability, chiefly an increase in ion pair number and the, considerable stabilisation of a mobile region seen in S. lividans CelB2., Additional aromatic residues in the active site region may also contribute, to the difference in thermophilicity.
About this Structure
1H0B 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
The structure of Rhodothermus marinus Cel12A, a highly thermostable family 12 endoglucanase, at 1.8 A resolution., Crennell SJ, Hreggvidsson GO, Nordberg Karlsson E, J Mol Biol. 2002 Jul 19;320(4):883-97. PMID:12095262
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