4ptd: Difference between revisions
New page: left|200px<br /> <applet load="4ptd" size="450" color="white" frame="true" align="right" spinBox="true" caption="4ptd, resolution 2.3Å" /> '''PHOSPHATIDYLINOSITOL... |
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==About this Structure== | ==About this Structure== | ||
4PTD is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.10 3.1.4.10]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4PTD OCA]]. | 4PTD is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]]. Active as [[http://en.wikipedia.org/wiki/Transferred_entry:_4.6.1.13 Transferred entry: 4.6.1.13]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.10 3.1.4.10]]. Structure known Active Site: ACT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4PTD OCA]]. | ||
==Reference== | ==Reference== | ||
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[[Category: Bacillus cereus]] | [[Category: Bacillus cereus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Transferred entry: 4.6.1.13]] | |||
[[Category: Heinz, D.W.]] | [[Category: Heinz, D.W.]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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[[Category: phosphoric diester]] | [[Category: phosphoric diester]] | ||
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Revision as of 13:21, 30 October 2007
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PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C MUTANT D274N
OverviewOverview
The role of amino acid residues located in the active site pocket of, phosphatidylinositol-specific phospholipase C (PI-PLC) from Bacillus, cereus[Heinz, D. W., Ryan, M., Bullock, T., & Griffith, O. H. (1995) EMBO, J. 14, 3855-3863] was investigated by site-directed mutagenesis, kinetics, and crystal structure analysis. Twelve residues involved in catalysis and, substrate binding (His32, Arg69, His82, Gly83, Lys115, Glu117, Arg163, Trp178, Asp180, Asp198, Tyr200, and Asp274) were individually replaced by, 1-3 other amino acids, resulting in a total number of 21 mutants., Replacements in the mutants H32A, H32L, R69A, R69E, R69K, H82A, H82L, E117K, R163I, D198A, D198E, D198S, Y200S, and D274S caused essentially, complete inactivation of the enzyme. The remaining mutants (G83S, K115E, ... [(full description)]
About this StructureAbout this Structure
4PTD is a [Single protein] structure of sequence from [Bacillus cereus]. Active as [Transferred entry: 4.6.1.13], with EC number [3.1.4.10]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
ReferenceReference
Probing the roles of active site residues in phosphatidylinositol-specific phospholipase C from Bacillus cereus by site-directed mutagenesis., Gassler CS, Ryan M, Liu T, Griffith OH, Heinz DW, Biochemistry. 1997 Oct 21;36(42):12802-13. PMID:9335537
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