1c9e

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(New page: 200px<br /><applet load="1c9e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c9e, resolution 2.30&Aring;" /> '''STRUCTURE OF FERROCH...)
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[[Image:1c9e.gif|left|200px]]<br /><applet load="1c9e" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1c9e, resolution 2.30&Aring;" />
 
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'''STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE'''<br />
 
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==Overview==
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==STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE==
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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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<StructureSection load='1c9e' size='340' side='right'caption='[[1c9e]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1c9e]] 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=1C9E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C9E FirstGlance]. <br>
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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]] 2.3&#8491;</td></tr>
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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>, <scene name='pdbligand=MP1:N-METHYLMESOPORPHYRIN+CONTAINING+COPPER'>MP1</scene></td></tr>
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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=1c9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c9e OCA], [https://pdbe.org/1c9e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c9e RCSB], [https://www.ebi.ac.uk/pdbsum/1c9e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c9e 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/c9/1c9e_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=1c9e ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1C9E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with MG and MP1 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C9E OCA].
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*[[Ferrochelatase 3D structures|Ferrochelatase 3D structures]]
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== References ==
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==Reference==
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<references/>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10704318 10704318]
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__TOC__
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</StructureSection>
[[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 MN]]
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[[Category: Fodje, M.N.]]
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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: MP1]]
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[[Category: bacillus subtilis]]
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[[Category: chelatase]]
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[[Category: heme synthesis]]
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[[Category: lyase]]
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[[Category: n-methylmesoporphyrin]]
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[[Category: porphyrin metallation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:16:52 2007''
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Current revision

STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE

PDB ID 1c9e

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