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1h6n

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[[Image:1h6n.gif|left|200px]]
[[Image:1h6n.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1h6n |SIZE=350|CAPTION= <scene name='initialview01'>1h6n</scene>, resolution 2.11&Aring;
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The line below this paragraph, containing "STRUCTURE_1h6n", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=HEM:Hem+Binding+Site+For+Chain+A+HIS+A+54+Is+The+Distal+HIS+...'>HEM</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OMT:S-DIOXYMETHIONINE'>OMT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= KATA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=584 Proteus mirabilis])
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-->
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|DOMAIN=
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{{STRUCTURE_1h6n| PDB=1h6n | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h6n OCA], [http://www.ebi.ac.uk/pdbsum/1h6n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h6n RCSB]</span>
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}}
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'''FORMATION OF A TYROSYL RADICAL INTERMEDIATE IN PROTEUS MIRABILIS CATALASE BY DIRECTED MUTAGENESIS AND CONSEQUENCES FOR NUCLEOTIDE REACTIVITY'''
'''FORMATION OF A TYROSYL RADICAL INTERMEDIATE IN PROTEUS MIRABILIS CATALASE BY DIRECTED MUTAGENESIS AND CONSEQUENCES FOR NUCLEOTIDE REACTIVITY'''
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[[Category: Jouve, H M.]]
[[Category: Jouve, H M.]]
[[Category: Sainz, G.]]
[[Category: Sainz, G.]]
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[[Category: hem]]
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[[Category: Hem]]
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[[Category: hydrogen peroxide]]
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[[Category: Hydrogen peroxide]]
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[[Category: iron]]
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[[Category: Iron]]
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[[Category: nadp]]
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[[Category: Nadp]]
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[[Category: oxidoreductase (h2o2 acceptor)]]
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[[Category: Peroxidase]]
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[[Category: peroxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:30:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:58:51 2008''
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Revision as of 15:30, 2 May 2008

Image:1h6n.gif

Template:STRUCTURE 1h6n

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 wild-type PMC, and it is surprising that the absence of iron had no effect on the structure of the active site. Met 53 close to the essential His 54 was found less oxidized in rec PMC than in the wild-type enzyme. An acetate anion was modeled in an anionic pocket, away from the heme group but important for the enzymatic reaction. An alternate conformation observed for Arg 99 could play a role in the formation of the H-bond network connecting two symmetrical subunits of the tetramer.

About this Structure

1H6N is a Single protein structure of sequence from Proteus mirabilis. 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 Page seeded by OCA on Fri May 2 18:30:02 2008

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