1oa2: Difference between revisions
New page: left|200px<br /> <applet load="1oa2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oa2, resolution 1.5Å" /> '''COMPARISON OF FAMILY... |
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==About this Structure== | ==About this Structure== | ||
1OA2 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ | 1OA2 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina]] with NAG 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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OA2 OCA]]. | ||
==Reference== | ==Reference== | ||
Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability., Sandgren M, Gualfetti PJ, Shaw A, Gross LS, Saldajeno M, Day AG, Jones TA, Mitchinson C, Protein Sci. 2003 Apr;12(4):848-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12649442 12649442] | Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability., Sandgren M, Gualfetti PJ, Shaw A, Gross LS, Saldajeno M, Day AG, Jones TA, Mitchinson C, Protein Sci. 2003 Apr;12(4):848-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12649442 12649442] | ||
[[Category: Cellulase]] | |||
[[Category: Hypocrea jecorina]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Day, A.G.]] | [[Category: Day, A.G.]] | ||
[[Category: Gross, L.S.]] | [[Category: Gross, L.S.]] | ||
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[[Category: trichoderma reesei cel12a]] | [[Category: trichoderma reesei cel12a]] | ||
''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 12:53:59 2007'' | ||
Revision as of 13:49, 30 October 2007
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COMPARISON OF FAMILY 12 GLYCOSIDE HYDROLASES AND RECRUITED SUBSTITUTIONS IMPORTANT FOR THERMAL STABILITY
OverviewOverview
As part of a program to discover improved glycoside hydrolase family 12, (GH 12) endoglucanases, we have studied the biochemical diversity of, several GH 12 homologs. The H. schweinitzii Cel12A enzyme differs from the, T. reesei Cel12A enzyme by only 14 amino acids (93% sequence identity), but is much less thermally stable. The bacterial Cel12A enzyme from S. sp., 11AG8 shares only 28% sequence identity to the T. reesei enzyme, and is, much more thermally stable. Each of the 14 sequence differences from H., schweinitzii Cel12A were introduced in T. reesei Cel12A to determine the, effect of these amino acid substitutions on enzyme stability. Several of, the T. reesei Cel12A variants were found to have increased stability, and, the differences in apparent midpoint of thermal denaturation ... [(full description)]
About this StructureAbout this Structure
1OA2 is a [Single protein] structure of sequence from [Hypocrea jecorina] with NAG as [ligand]. Active as [Cellulase], with EC number [3.2.1.4]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability., Sandgren M, Gualfetti PJ, Shaw A, Gross LS, Saldajeno M, Day AG, Jones TA, Mitchinson C, Protein Sci. 2003 Apr;12(4):848-60. PMID:12649442
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