1e93
From Proteopedia
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| - | [[Image:1e93.gif|left|200px]]<br /><applet load="1e93" size=" | + | [[Image:1e93.gif|left|200px]]<br /><applet load="1e93" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1e93, resolution 2.00Å" /> | caption="1e93, resolution 2.00Å" /> | ||
'''HIGH RESOLUTION STRUCTURE AND BIOCHEMICAL PROPERTIES OF A RECOMBINANT CATALASE DEPLETED IN IRON'''<br /> | '''HIGH RESOLUTION STRUCTURE AND BIOCHEMICAL PROPERTIES OF A RECOMBINANT CATALASE DEPLETED IN IRON'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1E93 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] Known structural/functional Site: <scene name='pdbsite=HEM:Hem Binding Site For Chain A HIS A 54 Is The Distal HIS ...'>HEM</scene>. Full crystallographic information is available from [http:// | + | 1E93 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 <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=HEM:'>HEM</scene> 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] Known structural/functional Site: <scene name='pdbsite=HEM:Hem+Binding+Site+For+Chain+A+HIS+A+54+Is+The+Distal+HIS+...'>HEM</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E93 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: peroxidase]] | [[Category: peroxidase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:38:21 2008'' |
Revision as of 07:38, 3 February 2008
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HIGH RESOLUTION STRUCTURE AND BIOCHEMICAL PROPERTIES OF A RECOMBINANT CATALASE DEPLETED IN IRON
Overview
Various enzymes use semi-stable ferryl intermediates and free radicals, during their catalytic cycle, amongst them haem catalases. Structures for, two transient intermediates (compounds I and II) of the NADPH-dependent, catalase from Proteus mirabilis (PMC) have been determined by, time-resolved X-ray crystallography and single crystal, microspectrophotometry. The results show the formation and transformation, of the ferryl group in the haem, and the unexpected binding of an anion, during this reaction at a site distant from the haem.
About this Structure
1E93 is a Single protein structure of sequence from Proteus mirabilis with , and as ligands. Active as Catalase, with EC number 1.11.1.6 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy., Gouet P, Jouve HM, Williams PA, Andersson I, Andreoletti P, Nussaume L, Hajdu J, Nat Struct Biol. 1996 Nov;3(11):951-6. PMID:8901874
Page seeded by OCA on Sun Feb 3 09:38:21 2008
Categories: Catalase | Proteus mirabilis | Single protein | Andreoletti, P. | Gagnon, J. | Jacquinot, M. | Jouve, H.M. | Sainz, G. | ACT | HEM | SO4 | Hem | Hydrogen peroxide | Iron | Nadp | Oxidoreductase (h2o2 acceptor) | Peroxidase
