1ak1

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(New page: 200px<br /> <applet load="1ak1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ak1, resolution 1.9&Aring;" /> '''FERROCHELATASE FROM ...)
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[[Image:1ak1.gif|left|200px]]<br />
 
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<applet load="1ak1" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ak1, resolution 1.9&Aring;" />
 
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'''FERROCHELATASE FROM BACILLUS SUBTILIS'''<br />
 
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==Overview==
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==FERROCHELATASE FROM BACILLUS SUBTILIS==
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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, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9384565 (full description)]]
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<StructureSection load='1ak1' size='340' side='right'caption='[[1ak1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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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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</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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</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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==About this Structure==
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==See Also==
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1AK1 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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=1AK1 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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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9384565 9384565]
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__TOC__
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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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. subtilis]]
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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://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 19:25:46 2007''
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Current revision

FERROCHELATASE FROM BACILLUS SUBTILIS

PDB ID 1ak1

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