1e93: Difference between revisions
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|PDB= 1e93 |SIZE=350|CAPTION= <scene name='initialview01'>1e93</scene>, resolution 2.00Å | |PDB= 1e93 |SIZE=350|CAPTION= <scene name='initialview01'>1e93</scene>, resolution 2.00Å | ||
|SITE= <scene name='pdbsite=HEM:Hem+Binding+Site+For+Chain+A+HIS+A+54+Is+The+Distal+HIS+...'>HEM</scene> | |SITE= <scene name='pdbsite=HEM:Hem+Binding+Site+For+Chain+A+HIS+A+54+Is+The+Distal+HIS+...'>HEM</scene> | ||
|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand= | |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> | ||
|ACTIVITY= [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] | |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> | ||
|GENE= KATA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=584 Proteus mirabilis]) | |GENE= KATA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=584 Proteus mirabilis]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e93 OCA], [http://www.ebi.ac.uk/pdbsum/1e93 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e93 RCSB]</span> | |||
}} | }} | ||
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[[Category: Jouve, H M.]] | [[Category: Jouve, H M.]] | ||
[[Category: Sainz, G.]] | [[Category: Sainz, G.]] | ||
[[Category: hem]] | [[Category: hem]] | ||
[[Category: hydrogen peroxide]] | [[Category: hydrogen peroxide]] | ||
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[[Category: peroxidase]] | [[Category: peroxidase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:57:44 2008'' | ||
Revision as of 16:57, 30 March 2008
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| 1e93, resolution 2.00Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Sites: | HEM | ||||||||||||
| Ligands: | ACT, HEM, OMT, SO4 | ||||||||||||
| Gene: | KATA (Proteus mirabilis) | ||||||||||||
| Activity: | Catalase, with EC number 1.11.1.6 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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
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