1doz

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[[Image:1doz.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF FERROCHELATASE==
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|PDB= 1doz |SIZE=350|CAPTION= <scene name='initialview01'>1doz</scene>, resolution 1.80&Aring;
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<StructureSection load='1doz' size='340' side='right'caption='[[1doz]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
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<table><tr><td colspan='2'>[[1doz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DOZ FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1doz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1doz OCA], [https://pdbe.org/1doz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1doz RCSB], [https://www.ebi.ac.uk/pdbsum/1doz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1doz ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CPFC_BACSU CPFC_BACSU] Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:25646457, PubMed:25908396). Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III (PubMed:25646457, PubMed:25908396). It can also insert iron into protoporphyrin IX (PubMed:1459957, PubMed:8119288, PubMed:21052751, PubMed:25646457). Has weaker activity with 2,4 disulfonate, deuteroporphyrin and 2,4 hydroxyethyl (PubMed:25646457, PubMed:12761666). In vitro, can also use Zn(2+) or Cu(2+) (PubMed:8119288, PubMed:16140324, PubMed:21052751, PubMed:12761666).<ref>PMID:12761666</ref> <ref>PMID:1459957</ref> <ref>PMID:16140324</ref> <ref>PMID:21052751</ref> <ref>PMID:25646457</ref> <ref>PMID:25826316</ref> <ref>PMID:25908396</ref> <ref>PMID:8119288</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/do/1doz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1doz ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF FERROCHELATASE'''
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==See Also==
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*[[Ferrochelatase 3D structures|Ferrochelatase 3D structures]]
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== References ==
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==Overview==
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<references/>
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Ferrochelatase, the enzyme catalyzing metallation of protoporphyrin IX at the terminal step of heme biosynthesis, was co-crystallized with an isomer mixture of the potent inhibitor N-methylmesoporphyrin (N-MeMP). The X-ray structure revealed the active site of the enzyme, to which only one of the isomers was bound, and for the first time allowed characterization of the mode of porphyrin macrocycle distortion by ferrochelatase. Crystallization of ferrochelatase and N-MeMP in the presence of Cu(2+) leads to metallation and demethylation of N-MeMP. A mechanism of porphyrin distortion is proposed, which assumes that the enzyme holds pyrrole rings B, C and D in a vice-like grip and forces a 36 degrees tilt on ring A.
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__TOC__
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</StructureSection>
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==About this Structure==
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1DOZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOZ OCA].
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==Reference==
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Structural and mechanistic basis of porphyrin metallation by ferrochelatase., Lecerof D, Fodje M, Hansson A, Hansson M, Al-Karadaghi S, J Mol Biol. 2000 Mar 17;297(1):221-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10704318 10704318]
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Ferrochelatase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Al-Karadaghi S]]
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[[Category: Al-Karadaghi, S.]]
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[[Category: Fodje M]]
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[[Category: Fodje, M.]]
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[[Category: Hansson A]]
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[[Category: Hansson, A.]]
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[[Category: Hansson M]]
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[[Category: Hansson, M.]]
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[[Category: Lecerof D]]
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[[Category: Lecerof, D.]]
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[[Category: MG]]
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[[Category: pi-helix]]
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[[Category: rossman fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:41:57 2008''
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Current revision

CRYSTAL STRUCTURE OF FERROCHELATASE

PDB ID 1doz

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