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- | {{Seed}} | |
- | [[Image:1c1h.png|left|200px]] | |
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- | <!-- | + | ==CRYSTAL STRUCTURE OF BACILLUS SUBTILIS FERROCHELATASE IN COMPLEX WITH N-METHYL MESOPORPHYRIN== |
- | The line below this paragraph, containing "STRUCTURE_1c1h", creates the "Structure Box" on the page.
| + | <StructureSection load='1c1h' size='340' side='right'caption='[[1c1h]], [[Resolution|resolution]] 1.90Å' scene=''> |
- | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | + | <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> |
- | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
- | -->
| + | <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> |
- | {{STRUCTURE_1c1h| PDB=1c1h | SCENE= }}
| + | <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> |
| + | </table> |
| + | == Function == |
| + | [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> |
| + | == Evolutionary Conservation == |
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> |
| + | <jmolCheckbox> |
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c1/1c1h_consurf.spt"</scriptWhenChecked> |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| + | </jmolCheckbox> |
| + | </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]. |
| + | <div style="clear:both"></div> |
| | | |
- | ===CRYSTAL STRUCTURE OF BACILLUS SUBTILIS FERROCHELATASE IN COMPLEX WITH N-METHYL MESOPORPHYRIN=== | + | ==See Also== |
- | | + | *[[Ferrochelatase|Ferrochelatase]] |
- | | + | *[[Ferrochelatase 3D structures|Ferrochelatase 3D structures]] |
- | <!--
| + | == References == |
- | The line below this paragraph, {{ABSTRACT_PUBMED_10704318}}, adds the Publication Abstract to the page
| + | <references/> |
- | (as it appears on PubMed at http://www.pubmed.gov), where 10704318 is the PubMed ID number.
| + | __TOC__ |
- | -->
| + | </StructureSection> |
- | {{ABSTRACT_PUBMED_10704318}}
| + | |
- | | + | |
- | ==About this Structure==
| + | |
- | 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].
| + | |
- | | + | |
- | ==Reference== | + | |
- | 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]
| + | |
| [[Category: Bacillus subtilis]] | | [[Category: Bacillus subtilis]] |
- | [[Category: Ferrochelatase]] | + | [[Category: Large Structures]] |
- | [[Category: Single protein]]
| + | [[Category: Al-Karadaghi S]] |
- | [[Category: Al-Karadaghi, S.]] | + | [[Category: Fodje M]] |
- | [[Category: Fodje, M.]] | + | [[Category: Hansson A]] |
- | [[Category: Hansson, A.]] | + | [[Category: Hansson M]] |
- | [[Category: Hansson, M.]] | + | [[Category: Lecerof D]] |
- | [[Category: Lecerof, D.]] | + | |
- | [[Category: Alpha/beta fold]]
| + | |
- | [[Category: Ferrochelatase]]
| + | |
- | [[Category: Heme synthesis]]
| + | |
- | [[Category: Pi-helix]]
| + | |
- | [[Category: Porphyrin metallation]]
| + | |
- | [[Category: Rossmann fold]]
| + | |
- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:04:47 2008''
| + | |
| Structural highlights
Function
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).[1] [2] [3] [4] [5] [6] [7] [8]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Lecerof D, Fodje MN, Alvarez Leon R, Olsson U, Hansson A, Sigfridsson E, Ryde U, Hansson M, Al-Karadaghi S. Metal binding to Bacillus subtilis ferrochelatase and interaction between metal sites. J Biol Inorg Chem. 2003 Apr;8(4):452-8. Epub 2003 Jan 18. PMID:12761666 doi:10.1007/s00775-002-0436-1
- ↑ Hansson M, Hederstedt L. Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes. J Bacteriol. 1992 Dec;174(24):8081-93. PMID:1459957 doi:10.1128/jb.174.24.8081-8093.1992
- ↑ Shipovskov S, Karlberg T, Fodje M, Hansson MD, Ferreira GC, Hansson M, Reimann CT, Al-Karadaghi S. Metallation of the transition-state inhibitor N-methyl mesoporphyrin by ferrochelatase: implications for the catalytic reaction mechanism. J Mol Biol. 2005 Oct 7;352(5):1081-90. PMID:16140324 doi:10.1016/j.jmb.2005.08.002
- ↑ Hansson MD, Karlberg T, Soderberg CA, Rajan S, Warren MJ, Al-Karadaghi S, Rigby SE, Hansson M. Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase. J Biol Inorg Chem. 2010 Nov 4. PMID:21052751 doi:10.1007/s00775-010-0720-4
- ↑ Dailey HA, Gerdes S, Dailey TA, Burch JS, Phillips JD. Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin. Proc Natl Acad Sci U S A. 2015 Feb 17;112(7):2210-5. PMID:25646457 doi:10.1073/pnas.1416285112
- ↑ Mielcarek A, Blauenburg B, Miethke M, Marahiel MA. Molecular insights into frataxin-mediated iron supply for heme biosynthesis in Bacillus subtilis. PLoS One. 2015 Mar 31;10(3):e0122538. PMID:25826316 doi:10.1371/journal.pone.0122538
- ↑ Lobo SA, Scott A, Videira MA, Winpenny D, Gardner M, Palmer MJ, Schroeder S, Lawrence AD, Parkinson T, Warren MJ, Saraiva LM. Staphylococcus aureus haem biosynthesis: characterisation of the enzymes involved in final steps of the pathway. Mol Microbiol. 2015 Aug;97(3):472-87. PMID:25908396 doi:10.1111/mmi.13041
- ↑ Hansson M, Hederstedt L. Purification and characterisation of a water-soluble ferrochelatase from Bacillus subtilis. Eur J Biochem. 1994 Feb 15;220(1):201-8. PMID:8119288 doi:10.1111/j.1432-1033.1994.tb18615.x
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