7x98

5-Aminolevulinate synthase HemA from Rhodopseudomonas palustris

spinqualitylabelsall models 7x98, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7x98 is a 4 chain structure with sequence from Rhodopseudomonas palustris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.05Å Ligands: LLP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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