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[[Image:3lgn.png|left|200px]]


{{STRUCTURE_3lgn| PDB=3lgn | SCENE= }}
==Crystal structure of IsdI in complex with heme==
<StructureSection load='3lgn' size='340' side='right'caption='[[3lgn]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3lgn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_N315 Staphylococcus aureus subsp. aureus N315]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LGN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LGN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3lgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lgn OCA], [https://pdbe.org/3lgn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lgn RCSB], [https://www.ebi.ac.uk/pdbsum/3lgn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lgn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HDOX2_STAAN HDOX2_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.[HAMAP-Rule:MF_01272]<ref>PMID:18713745</ref> <ref>PMID:20180905</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lg/3lgn_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lgn ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enzymatic haem catabolism by haem oxygenases is conserved from bacteria to humans and proceeds through a common mechanism leading to the formation of iron, carbon monoxide and biliverdin. The first members of a novel class of haem oxygenases were recently identified in Staphylococcus aureus (IsdG and IsdI) and were termed the IsdG-family of haem oxygenases. Enzymes of the IsdG-family form tertiary structures distinct from those of the canonical haem oxygenase family, suggesting that IsdG-family members degrade haem via a unique reaction mechanism. Herein we report that the IsdG-family of haem oxygenases degrade haem to the oxo-bilirubin chromophore staphylobilin. We also present the crystal structure of haem-bound IsdI in which haem ruffling and constrained binding of oxygen is consistent with cleavage of the porphyrin ring at the beta- or delta-meso carbons. Combined, these data establish that the IsdG-family of haem oxygenases degrades haem to a novel chromophore distinct from biliverdin.


===Crystal structure of IsdI in complex with heme===
The IsdG-family of haem oxygenases degrades haem to a novel chromophore.,Reniere ML, Ukpabi GN, Harry SR, Stec DF, Krull R, Wright DW, Bachmann BO, Murphy ME, Skaar EP Mol Microbiol. 2010 Mar;75(6):1529-38. Epub 2010 Feb 17. PMID:20180905<ref>PMID:20180905</ref>


{{ABSTRACT_PUBMED_20180905}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 3lgn" style="background-color:#fffaf0;"></div>
[[3lgn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LGN OCA].


==See Also==
==See Also==
*[[Heme oxygenase|Heme oxygenase]]
*[[Heme oxygenase 3D structures|Heme oxygenase 3D structures]]
 
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
==Reference==
== References ==
<ref group="xtra">PMID:020180905</ref><references group="xtra"/>
<references/>
[[Category: Heme oxygenase]]
__TOC__
[[Category: Staphylococcus aureus]]
</StructureSection>
[[Category: Murphy, M E.P.]]
[[Category: Large Structures]]
[[Category: Ukpabi, G N.]]
[[Category: Staphylococcus aureus subsp. aureus N315]]
[[Category: Dimeric alpha+beta barrel]]
[[Category: Murphy MEP]]
[[Category: Heme]]
[[Category: Ukpabi GN]]
[[Category: Iron]]
[[Category: Metal-binding]]
[[Category: Monooxygenase]]
[[Category: Oxidoreductase]]
Retrieved from "https://proteopedia.org/3lgn"