5YKR

Crystal structure of a glutamate-1-semialdehyde-aminomutase from Pseudomonas aeruginosa PAO1

Summary for 5YKR

• Entry DOI: 10.2210/pdb5ykr/pdb
• Descriptor: Probable aminotransferase (2 entities in total)
• Functional Keywords: glutamate-1-semialdehyde-aminomutase, c5 pathway, transferase
• Biological source: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
• Total number of polymer chains: 2
• Total formula weight: 102630.23

Authors

Li, S.,Zhang, Q.,Bartlam, M. (deposition date: 2017-10-16, release date: 2018-09-26, Last modification date: 2023-11-22)

Primary citation

Li, S.,Lou, X.,Xu, Y.,Teng, X.,Che, S.,Liu, R.,Bartlam, M.
Crystal structure of a glutamate-1-semialdehyde-aminomutase from Pseudomonas aeruginosa PAO1.
Biochem. Biophys. Res. Commun., 500:804-809, 2018

PubMed Abstract: The C5 pathway in bacteria is responsible for the synthesis of 5-aminolevulinic acid, which forms the core skeleton of cofactors required for metabolism. One of the key actors in this pathway is a pyridoxamine-5'-phosphate (PMP)/pyridoxal-5'-phosphate (PLP) dependent enzyme called glutamate-1-semialdehyde aminomutase (GSAM). In this study, we crystallized the expression product of the uncharacterized pa4088 gene from the opportunistic pathogen Pseudomonas aeruginosa PAO1. The resulting high-resolution structure confirms it to be a member of the GSAM family. Continuous electron density indicates the presence of a PLP cofactor with a Schiff base linkage between the PLP cofactor and the ε-amino group of Lys286. A crystal structure of a K286A mutant in complex with PMP is also reported. As GSAM enzymes are not present in mammalian cells, this work provides a starting point for the investigation of GSAM as a target for drug development against P. aeruginosa infection.

PubMed: 29684343
DOI: 10.1016/j.bbrc.2018.04.163

Experimental method

X-RAY DIFFRACTION (1.44 Å)