6p5z: Difference between revisions

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<StructureSection load='6p5z' size='340' side='right'caption='[[6p5z]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
<StructureSection load='6p5z' size='340' side='right'caption='[[6p5z]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6p5z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P5Z FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P5Z FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26&#8491;</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]] 2.26&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=F0X:cobalt-sirohydrochlorin'>F0X</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=F0X:cobalt-sirohydrochlorin'>F0X</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></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=6p5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p5z OCA], [https://pdbe.org/6p5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p5z RCSB], [https://www.ebi.ac.uk/pdbsum/6p5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p5z 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=6p5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p5z OCA], [https://pdbe.org/6p5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p5z RCSB], [https://www.ebi.ac.uk/pdbsum/6p5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p5z ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CYSG_SALTY CYSG_SALTY] Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme.<ref>PMID:14595395</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Siroheme is the central cofactor in a conserved class of sulfite and nitrite reductases that catalyze the six-electron reduction of sulfite to sulfide and nitrite to ammonia. In Salmonella enterica serovar Typhimurium, siroheme is produced by a trifunctional enzyme, siroheme synthase (CysG). A bifunctional active site that is distinct from its methyltransferase activity catalyzes the final two steps, NAD(+)-dependent dehydrogenation and iron chelation. How this active site performs such different chemistries is unknown. Here, we report the structures of CysG bound to precorrin-2, the initial substrate; sirohydrochlorin, the dehydrogenation product/chelation substrate; and a cobalt-sirohydrochlorin product. We identified binding poses for all three tetrapyrroles and tested the roles of specific amino acids in both activities to give insights into how a bifunctional active site catalyzes two different chemistries and acts as an iron-specific chelatase in the final step of siroheme synthesis.
Siroheme synthase orients substrates for dehydrogenase and chelatase activities in a common active site.,Pennington JM, Kemp M, McGarry L, Chen Y, Stroupe ME Nat Commun. 2020 Feb 13;11(1):864. doi: 10.1038/s41467-020-14722-1. PMID:32054833<ref>PMID:32054833</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6p5z" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Siroheme synthase|Siroheme synthase]]
*[[Siroheme synthase|Siroheme synthase]]
*[[3D structures of syntenin|3D structures of syntenin]]
*[[3D structures of syntenin|3D structures of syntenin]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Pennington JM]]
[[Category: Pennington JM]]
[[Category: Stroupe ME]]
[[Category: Stroupe ME]]

Latest revision as of 09:57, 25 December 2024

Cobalt-sirohydrochlorin-bound S. typhimurium siroheme synthase

6p5z, resolution 2.26Å

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