1ak1

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[[Image:1ak1.gif|left|200px]]
 
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==FERROCHELATASE FROM BACILLUS SUBTILIS==
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The line below this paragraph, containing "STRUCTURE_1ak1", creates the "Structure Box" on the page.
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<StructureSection load='1ak1' size='340' side='right'caption='[[1ak1]], [[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'>[[1ak1]] 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=1AK1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AK1 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ak1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ak1 OCA], [https://pdbe.org/1ak1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ak1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ak1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ak1 ProSAT]</span></td></tr>
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{{STRUCTURE_1ak1| PDB=1ak1 | SCENE= }}
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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/ak/1ak1_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=1ak1 ConSurf].
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<div style="clear:both"></div>
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'''FERROCHELATASE FROM BACILLUS SUBTILIS'''
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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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BACKGROUND: The metallation of closed ring tetrapyrroles resulting in the formation of hemes, chlorophylls and vitamin B12 is catalyzed by specific enzymes called chelatases. Ferrochelatase catalyzes the terminal step in heme biosynthesis by inserting ferrous ion into protoporphyrin IX by a mechanism that is poorly understood. Mutations in the human gene for ferrochelatase can result in the disease erythropoietic protoporphyria, and a further understanding of the mechanism of this enzyme is therefore of clinical interest. No three-dimensional structure of a tetrapyrrole metallation enzyme has been available until now. Results: The three-dimensional structure of Bacillus subtilis ferrochelatase has been determined at 1.9 A resolution by the method of multiple isomorphous replacement. The structural model contains 308 of the 310 amino acid residues of the protein and 198 solvent molecules. The polypeptide is folded into two similar domains each with a four-stranded parallel beta sheet flanked by alpha helices. Structural elements from both domains build up a cleft, which contains several amino acid residues that are invariant in ferrochelatases from different organisms. In crystals soaked with gold and cadmium salt solutions, the metal ion was found to be coordinated to the conserved residue His 183, which is located in the cleft. This histidine residue has previously been suggested to be involved in ferrous ion binding. CONCLUSIONS: Ferrochelatase seems to have a structurally conserved core region that is common to the enzyme from bacteria, plants and mammals. We propose that porphyrin binds in the identified cleft; this cleft also includes the metal-binding site of the enzyme. It is likely that the structure of the cleft region will have different conformations upon substrate binding and release.
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__TOC__
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</StructureSection>
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==About this Structure==
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1AK1 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=1AK1 OCA].
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==Reference==
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Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis., Al-Karadaghi S, Hansson M, Nikonov S, Jonsson B, Hederstedt L, Structure. 1997 Nov 15;5(11):1501-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9384565 9384565]
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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: Hansson M]]
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[[Category: Hansson, M.]]
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[[Category: Hederstedt L]]
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[[Category: Hederstedt, L.]]
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[[Category: Jonsson B]]
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[[Category: Jonsson, B.]]
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[[Category: Nikonov S]]
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[[Category: Nikonov, S.]]
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[[Category: B. subtili]]
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[[Category: Heme synthesis]]
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[[Category: Metallation]]
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[[Category: Porphyrin]]
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[[Category: Protoheme ferro-lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:22:12 2008''
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Current revision

FERROCHELATASE FROM BACILLUS SUBTILIS

PDB ID 1ak1

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