Structural highlights
Function
M1FRN3_RHOPL
Publication Abstract from PubMed
5-ALA is the precursor of all tetrapyrroles. 5-Aminolevulinate synthase (ALAS) catalyzes the production of 5-aminolevulinic acid (5-ALA) from glycine and succinyl-CoA. HemA from Rhodopseudomonas palustris (Rp-HemA) was reported to be a highly active ALAS. To understand the catalytic mechanism of Rp-HemA, the 2.05 A resolution crystal structure of Rp-HemA was solved. Open, half close and close conformations were observed in the substrate-free structures. Structure comparison and sequence alignment suggest the newly observed half close conformation may also be conserved in ALAS family. The pre-existed close and half close conformations in Rp-HemA may play a key role for its high activity.
Crystal structure of 5-Aminolevulinate synthase HemA from Rhodopseudomonas palustris presents multiple conformations.,Zhang T, Chen J, Zheng P, Gong W, Sun J, Liu H Biochem Biophys Res Commun. 2022 Jun 18;609:100-104. doi: , 10.1016/j.bbrc.2022.04.021. Epub 2022 Apr 9. PMID:35427926[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang T, Chen J, Zheng P, Gong W, Sun J, Liu H. Crystal structure of 5-Aminolevulinate synthase HemA from Rhodopseudomonas palustris presents multiple conformations. Biochem Biophys Res Commun. 2022 Jun 18;609:100-104. PMID:35427926 doi:10.1016/j.bbrc.2022.04.021
