3qgp
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qgp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qgp RCSB], [http://www.ebi.ac.uk/pdbsum/3qgp PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qgp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qgp RCSB], [http://www.ebi.ac.uk/pdbsum/3qgp PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ISDI_STAAN ISDI_STAAN]] Allows bacterial pathogens to use the host heme as an iron source. Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring to the oxo-bilirubin chromophore staphylobilin (a mixture of the linear tetrapyrroles 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin) in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron.<ref>PMID:18713745</ref> <ref>PMID:20180905</ref> | ||
==See Also== | ==See Also== | ||
*[[Heme oxygenase|Heme oxygenase]] | *[[Heme oxygenase|Heme oxygenase]] | ||
*[[Monooxygenase|Monooxygenase]] | *[[Monooxygenase|Monooxygenase]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 11:50, 25 December 2014
Crystal structure of IsdI in complex with heme and cyanide
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