1c1h

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[[Image:1c1h.jpg|left|200px]]
 
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==CRYSTAL STRUCTURE OF BACILLUS SUBTILIS FERROCHELATASE IN COMPLEX WITH N-METHYL MESOPORPHYRIN==
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The line below this paragraph, containing "STRUCTURE_1c1h", creates the "Structure Box" on the page.
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<StructureSection load='1c1h' size='340' side='right'caption='[[1c1h]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1c1h]] 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=1C1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C1H FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.9&#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=MMP:N-METHYLMESOPORPHYRIN'>MMP</scene></td></tr>
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{{STRUCTURE_1c1h| PDB=1c1h | SCENE= }}
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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=1c1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c1h OCA], [https://pdbe.org/1c1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c1h RCSB], [https://www.ebi.ac.uk/pdbsum/1c1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c1h 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/c1/1c1h_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=1c1h ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF BACILLUS SUBTILIS FERROCHELATASE IN COMPLEX WITH N-METHYL MESOPORPHYRIN'''
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==See Also==
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*[[Ferrochelatase|Ferrochelatase]]
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*[[Ferrochelatase 3D structures|Ferrochelatase 3D structures]]
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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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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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1C1H 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=1C1H 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: Alpha/beta fold]]
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[[Category: Ferrochelatase]]
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[[Category: Heme synthesis]]
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[[Category: Pi-helix]]
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[[Category: Porphyrin metallation]]
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[[Category: Rossmann fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:13:12 2008''
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Current revision

CRYSTAL STRUCTURE OF BACILLUS SUBTILIS FERROCHELATASE IN COMPLEX WITH N-METHYL MESOPORPHYRIN

PDB ID 1c1h

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