1h6n: Difference between revisions
New page: left|200px<br /> <applet load="1h6n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h6n, resolution 2.11Å" /> '''FORMATION OF A TYRO... |
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==About this Structure== | ==About this Structure== | ||
1H6N is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Proteus_mirabilis Proteus mirabilis]] with ACT, SO4 and HEM 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=1.11.1.6 1.11.1.6]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H6N OCA]]. | 1H6N is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Proteus_mirabilis Proteus mirabilis]] with ACT, SO4 and HEM as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Catalase Catalase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6]]. Structure known Active Site: HEM. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H6N OCA]]. | ||
==Reference== | ==Reference== | ||
High-resolution structure and biochemical properties of a recombinant Proteus mirabilis catalase depleted in iron., Andreoletti P, Sainz G, Jaquinod M, Gagnon J, Jouve HM, Proteins. 2003 Feb 1;50(2):261-71. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12486720 12486720] | High-resolution structure and biochemical properties of a recombinant Proteus mirabilis catalase depleted in iron., Andreoletti P, Sainz G, Jaquinod M, Gagnon J, Jouve HM, Proteins. 2003 Feb 1;50(2):261-71. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12486720 12486720] | ||
[[Category: Catalase]] | |||
[[Category: Proteus mirabilis]] | [[Category: Proteus mirabilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: peroxidase]] | [[Category: peroxidase]] | ||
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Revision as of 09:26, 30 October 2007
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FORMATION OF A TYROSYL RADICAL INTERMEDIATE IN PROTEUS MIRABILIS CATALASE BY DIRECTED MUTAGENESIS AND CONSEQUENCES FOR NUCLEOTIDE REACTIVITY
Overview
Heme catalases are homotetrameric enzymes with a highly conserved complex, quaternary structure, and their functional role is still not well, understood. Proteus mirabilis catalase (PMC), a heme enzyme belonging to, the family of NADPH-binding catalases, was efficiently overexpressed in E., coli. The recombinant catalase (rec PMC) was deficient in heme with, one-third heme and two-thirds protoporphyrin IX as determined by mass, spectrometry and chemical methods. This ratio was influenced by the, expression conditions, but the enzyme-specific activity calculated, relative to the heme content remained unchanged. The crystal structure of, rec PMC was solved to a resolution of 2.0 A, the highest resolution, obtained to date with PMC. The overall structure was quite similar to that, of ... [(full description)]
About this Structure
1H6N is a [Single protein] structure of sequence from [Proteus mirabilis] with ACT, SO4 and HEM as [ligands]. Active as [Catalase], with EC number [1.11.1.6]. Structure known Active Site: HEM. Full crystallographic information is available from [OCA].
Reference
High-resolution structure and biochemical properties of a recombinant Proteus mirabilis catalase depleted in iron., Andreoletti P, Sainz G, Jaquinod M, Gagnon J, Jouve HM, Proteins. 2003 Feb 1;50(2):261-71. PMID:12486720
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