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| | <StructureSection load='1l8x' size='340' side='right'caption='[[1l8x]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='1l8x' size='340' side='right'caption='[[1l8x]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1l8x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8X OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1L8X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1l8x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L8X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HEMZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l8x OCA], [https://pdbe.org/1l8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l8x RCSB], [https://www.ebi.ac.uk/pdbsum/1l8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l8x ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1l8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l8x OCA], [http://pdbe.org/1l8x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l8x RCSB], [http://www.ebi.ac.uk/pdbsum/1l8x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1l8x ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HEMH_YEAST HEMH_YEAST]] Catalyzes the ferrous insertion into protoporphyrin IX.[HAMAP-Rule:MF_00323] | + | [https://www.uniprot.org/uniprot/HEMH_YEAST HEMH_YEAST] Catalyzes the ferrous insertion into protoporphyrin IX.[HAMAP-Rule:MF_00323] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| - | [[Category: Ferrochelatase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Al-Karadaghi, S]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Gora, M]] | + | [[Category: Al-Karadaghi S]] |
| - | [[Category: Hansson, M]] | + | [[Category: Gora M]] |
| - | [[Category: Karlberg, T]] | + | [[Category: Hansson M]] |
| - | [[Category: Labbe-Bois, R]] | + | [[Category: Karlberg T]] |
| - | [[Category: Lecerof, D]] | + | [[Category: Labbe-Bois R]] |
| - | [[Category: Silvegren, G]] | + | [[Category: Lecerof D]] |
| - | [[Category: Cobalt]]
| + | [[Category: Silvegren G]] |
| - | [[Category: Ferro-lyase]]
| + | |
| - | [[Category: Heme biosynthesis]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Mitochondrial inner membrane protein]]
| + | |
| - | [[Category: Porphyrin metallation]]
| + | |
| - | [[Category: Protoheme]]
| + | |
| Structural highlights
Function
HEMH_YEAST Catalyzes the ferrous insertion into protoporphyrin IX.[HAMAP-Rule:MF_00323]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Ferrochelatase is the terminal enzyme in the heme biosynthetic pathway. It catalyzes the insertion of ferrous iron into protoporphyrin IX to produce protoheme IX. The crystal structures of ferrochelatase from Saccharomyces cerevisiae in free form, in complex with Co(II), a substrate metal ion, and in complex with two inhibitors, Cd(II) and Hg(I), are presented in this work. The enzyme is a homodimer, with clear asymmetry between the monomers with regard to the porphyrin binding cleft and the mode of metal binding. The Co(II) and Cd(II) complexes reveal the metal binding site which consists of the invariant amino acids H235, E314, and S275 and solvent molecules. The shortest distance to the metal reveals that amino acid H235 is the primary metal binding residue. A second site with bound Cd(II) was found close to the surface of the molecule, approximately 14 A from H235, with E97, H317, and E326 participating in metal coordination. It is suggested that this site corresponds to the magnesium binding site in Bacillus subtilis ferrochelatase. The latter site is also located at the surface of the molecule and thought to be involved in initial metal binding and regulation.
Metal binding to Saccharomyces cerevisiae ferrochelatase.,Karlberg T, Lecerof D, Gora M, Silvegren G, Labbe-Bois R, Hansson M, Al-Karadaghi S Biochemistry. 2002 Nov 19;41(46):13499-506. PMID:12427010[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Karlberg T, Lecerof D, Gora M, Silvegren G, Labbe-Bois R, Hansson M, Al-Karadaghi S. Metal binding to Saccharomyces cerevisiae ferrochelatase. Biochemistry. 2002 Nov 19;41(46):13499-506. PMID:12427010
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