7X98

5-Aminolevulinate synthase HemA from Rhodopseudomonas palustris

Summary for 7X98

• Entry DOI: 10.2210/pdb7x98/pdb
• Descriptor: 5-aminolevulinate synthase (2 entities in total)
• Functional Keywords: plp dependent enzyme, transferase
• Biological source: Rhodopseudomonas palustris
• Total number of polymer chains: 4
• Total formula weight: 175861.34

Authors

Zhang, T.T.,Liu, H.P. (deposition date: 2022-03-15, release date: 2023-03-08, Last modification date: 2023-11-29)

Primary citation

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., 609:100-104, 2022

PubMed 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.

PubMed: 35427926
DOI: 10.1016/j.bbrc.2022.04.021

Experimental method

X-RAY DIFFRACTION (2.05 Å)