Siroheme synthase: Difference between revisions
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
[[1pjq]] – StCysG + SAH – ''Salmonella typhimurium''<BR /> | |||
[[1pjt]], [[6p7c]], [[6p7d]], [[6pqz]], [[6pr0]], [[6pr1]], [[6pr2]], [[6pr3]], [[6pr4]], [[6ulu]] – StCysG (mutant) + SAH <BR /> | |||
[[6p5z]] – StCysG + SAH + Co-sirohydrochlorin <BR /> | |||
[[1pjs]] – StCysG + SAH + NAD <BR /> | |||
[[6p5x]] – StCysG (mutant) + SAH + substrate<BR /> | |||
[[6veb]] – StCysG (mutant) + SAH + NAD + pecorrin<BR /> | |||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Revision as of 13:34, 28 June 2022
FunctionSiroheme synthase (CysG) catalyzes the reduction of sulfite to sulfide or nitrite to ammonia[1]. CysG substrate is a tetrapyrrole. Structural highlightsThe tetrapyrrole in siroheme is heavily negatively charged because of the 8 acetyl and propionyl carboxylates at the corners of the siroheme and it interacts with residues of subunit #1 and subunit #2. Seven of these residues are positively charged Arg and Lys residues.
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Siroheme synthase 3D structuresSiroheme synthase 3D structures
Updated on 28-June-2022
1pjq – StCysG + SAH – Salmonella typhimurium
1pjt, 6p7c, 6p7d, 6pqz, 6pr0, 6pr1, 6pr2, 6pr3, 6pr4, 6ulu – StCysG (mutant) + SAH
6p5z – StCysG + SAH + Co-sirohydrochlorin
1pjs – StCysG + SAH + NAD
6p5x – StCysG (mutant) + SAH + substrate
6veb – StCysG (mutant) + SAH + NAD + pecorrin
ReferencesReferences
- ↑ Pennington JM, Kemp M, McGarry L, Chen Y, Stroupe ME. Siroheme synthase orients substrates for dehydrogenase and chelatase activities in a common active site. Nat Commun. 2020 Feb 13;11(1):864. doi: 10.1038/s41467-020-14722-1. PMID:32054833 doi:http://dx.doi.org/10.1038/s41467-020-14722-1