This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Siroheme synthase
From Proteopedia
| (2 intermediate revisions not shown.) | |||
| Line 7: | Line 7: | ||
== Structural highlights == | == Structural highlights == | ||
| - | The tetrapyrrole in siroheme is heavily negatively charged because of | + | The 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 <scene name='91/915831/Cv/6'>residues of subunits A and B</scene>. Five of these residues are positively charged <scene name='91/915831/Cv/7'>Arg and Lys residues</scene>. |
</StructureSection> | </StructureSection> | ||
Current revision
| |||||||||||
Siroheme synthase 3D structures
Updated on 03-July-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
References
- ↑ 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
