1a2q
From Proteopedia
(New page: 200px<br /> <applet load="1a2q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a2q, resolution 1.80Å" /> '''SUBTILISIN BPN' MUT...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1A2Q is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]] with CA and ACN 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=3.4.21.62 3.4.21.62]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A2Q OCA]]. | + | 1A2Q is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]] with CA and ACN as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Subtilisin Subtilisin]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62]]. Structure known Active Sites: 169, 218, C22, C87, CA1 and CA2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A2Q OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus amyloliquefaciens]] | [[Category: Bacillus amyloliquefaciens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| + | [[Category: Subtilisin]] | ||
[[Category: Gilliland, G.L.]] | [[Category: Gilliland, G.L.]] | ||
[[Category: Howard, A.J.]] | [[Category: Howard, A.J.]] | ||
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[[Category: sporulation]] | [[Category: sporulation]] | ||
| - | ''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 12:08:31 2007'' |
Revision as of 10:03, 30 October 2007
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SUBTILISIN BPN' MUTANT 7186
Overview
Six individual amino acid substitutions at separate positions in the, tertiary structure of subtilisin BPN' (EC 3.4.21.14) were found to, increase the stability of this enzyme, as judged by differential scanning, calorimetry and decreased rates of thermal inactivation. These stabilizing, changes, N218S, G169A, Y217K, M50F, Q206C, and N76D, were discovered, through the use of five different investigative approaches: (1) random, mutagenesis; (2) design of buried hydrophobic side groups; (3) design of, electrostatic interactions at Ca2+ binding sites; (4) sequence homology, consensus; and (5) serendipity. Individually, the six amino acid, substitutions increase the delta G of unfolding between 0.3 and 1.3, kcal/mol at 58.5 degrees C. The combination of these six individual, stabilizing ... [(full description)]
About this Structure
1A2Q is a [Single protein] structure of sequence from [Bacillus amyloliquefaciens] with CA and ACN as [ligands]. Active as [Subtilisin], with EC number [3.4.21.62]. Structure known Active Sites: 169, 218, C22, C87, CA1 and CA2. Full crystallographic information is available from [OCA].
Reference
Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding., Pantoliano MW, Whitlow M, Wood JF, Dodd SW, Hardman KD, Rollence ML, Bryan PN, Biochemistry. 1989 Sep 5;28(18):7205-13. PMID:2684274
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