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Siroheme synthase
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | 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>. | + | 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
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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
