Crystal structure of 5-Aminolevulinate synthase HemA from Rhodopseudomonas palustris presents multiple conformations

Biochem Biophys Res Commun. 2022 Jun 18:609:100-104. doi: 10.1016/j.bbrc.2022.04.021. Epub 2022 Apr 9.

Abstract

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 Å 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.

Keywords: 5-Aminolevulinate synthase; Crystal structure; Glycine; Pyridoxal 5′-phosphate; Succinyl-CoA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 5-Aminolevulinate Synthetase* / chemistry
  • Aminolevulinic Acid
  • Glycine
  • Rhodopseudomonas*

Substances

  • Aminolevulinic Acid
  • 5-Aminolevulinate Synthetase
  • Glycine

Supplementary concepts

  • Rhodopseudomonas palustris