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| | <StructureSection load='6rwv' size='340' side='right'caption='[[6rwv]], [[Resolution|resolution]] 1.64Å' scene=''> | | <StructureSection load='6rwv' size='340' side='right'caption='[[6rwv]], [[Resolution|resolution]] 1.64Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6rwv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RWV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RWV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6rwv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RWV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.6386379Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6rwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rwv OCA], [http://pdbe.org/6rwv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rwv RCSB], [http://www.ebi.ac.uk/pdbsum/6rwv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rwv ProSAT]</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=6rwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rwv OCA], [https://pdbe.org/6rwv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rwv RCSB], [https://www.ebi.ac.uk/pdbsum/6rwv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rwv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A3T2BSC5_LISMN A0A3T2BSC5_LISMN]] Catalyzes the ferrous insertion into protoporphyrin IX.[HAMAP-Rule:MF_00323][RuleBase:RU000607][SAAS:SAAS00982004] | + | [https://www.uniprot.org/uniprot/CPFC_LISMO CPFC_LISMO] Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:31794133). Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III (PubMed:31794133).<ref>PMID:31794133</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6rwv" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6rwv" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ferrochelatase 3D structures|Ferrochelatase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ferrochelatase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Djinovic-Carugo, K]] | + | [[Category: Listeria monocytogenes]] |
| - | [[Category: Furtmueller, P G]] | + | [[Category: Djinovic-Carugo K]] |
| - | [[Category: Helm, J]] | + | [[Category: Furtmueller PG]] |
| - | [[Category: Hofbauer, S]] | + | [[Category: Helm J]] |
| - | [[Category: Ferredoxin-like fold]]
| + | [[Category: Hofbauer S]] |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Prokaryotic heme biosynthesis]]
| + | |
| Structural highlights
Function
CPFC_LISMO Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:31794133). Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III (PubMed:31794133).[1]
Publication Abstract from PubMed
Coproporphyrin ferrochelatases (CpfCs, EC 4.99.1.9) insert ferrous iron into coproporphyrin III yielding coproheme. CpfCs are utilized by prokaryotic, mainly monoderm (Gram-positive) bacteria within the recently detected coproporphyrin-dependent heme biosynthesis pathway. Here we present a comprehensive study on CpfC from Listeria monocytogenes (LmCpfC) including the first crystal structure of a coproheme-bound CpfC. Comparison of crystal structures of apo-LmCpfC and coproheme-LmCpfC allowed identification of structural rearrangements and of amino acids involved in tetrapyrrole macrocycle and Fe(2+) binding. Differential scanning calorimetry of apo-, coproporphyrin III- and coproheme-LmCpfC underline the pronounced non-covalent interaction of both coproporphyrin and coproheme with the protein (DeltaTm = 11 degrees C compared to apo-LmCpfC) which includes the propionates (p2, p4, p6, p7) and the amino acids Arg29, Arg45, Tyr46, Ser53 and Tyr124. Furthermore, the thermodynamics and kinetics of coproporphyrin III and coproheme binding to apo-LmCpfC is presented as well as the kinetics of insertion of ferrous iron into coproporphyrin III-LmCpfC that immediately leads to formation of ferric coproheme-LmCpfC (kcat /KM = 4.7 x 10(5) M(-1) s(-1) ). We compare the crystal structure of coproheme-LmCpfC with available structures of CpfCs with artificial tetrapyrrole macrocycles and discuss our data on substrate binding, iron insertion and substrate release in the context of the coproporphyrin-dependent heme biosynthesis pathway.
Crystal structures and calorimetry reveal catalytically relevant binding mode of coproporphyrin and coproheme in coproporphyrin ferrochelatase.,Hofbauer S, Helm J, Obinger C, Djinovic-Carugo K, Furtmuller PG FEBS J. 2019 Dec 3. doi: 10.1111/febs.15164. PMID:31794133[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hofbauer S, Helm J, Obinger C, Djinovic-Carugo K, Furtmuller PG. Crystal structures and calorimetry reveal catalytically relevant binding mode of coproporphyrin and coproheme in coproporphyrin ferrochelatase. FEBS J. 2019 Dec 3. doi: 10.1111/febs.15164. PMID:31794133 doi:http://dx.doi.org/10.1111/febs.15164
- ↑ Hofbauer S, Helm J, Obinger C, Djinovic-Carugo K, Furtmuller PG. Crystal structures and calorimetry reveal catalytically relevant binding mode of coproporphyrin and coproheme in coproporphyrin ferrochelatase. FEBS J. 2019 Dec 3. doi: 10.1111/febs.15164. PMID:31794133 doi:http://dx.doi.org/10.1111/febs.15164
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