6A2F

Crystal structure of biosynthetic alanine racemase from Pseudomonas aeruginosa

Summary for 6A2F

• Entry DOI: 10.2210/pdb6a2f/pdb
• Descriptor: Alanine racemase, biosynthetic, MALONATE ION, D-LYSINE, ... (5 entities in total)
• Functional Keywords: alanine racemase, alr, pseudomonas aeruginosa, l-alanine, d-alanine, isomerase
• Biological source: Pseudomonas aeruginosa PAO1
• Total number of polymer chains: 2
• Total formula weight: 77780.46

Authors

Dong, H.,Li, S. (deposition date: 2018-06-11, release date: 2018-08-08, Last modification date: 2023-11-22)

Primary citation

Dong, H.,Han, Q.,Guo, Y.,Ju, J.,Wang, S.,Yuan, C.,Long, W.,He, X.,Xu, S.,Li, S.
Enzymatic characterization and crystal structure of biosynthetic alanine racemase from Pseudomonas aeruginosa PAO1.
Biochem.Biophys.Res.Commun., 503:2319-2325, 2018

PubMed Abstract: Alanine racemase is a pyridoxal-5'-phosphate (PLP)-dependent enzyme that reversibly catalyzes the conversion of l-alanine to d-alanine. d-alanine is an essential constituent in many prokaryotic cell structures. Inhibition of alanine racemase is lethal to prokaryotes, creating an attractive target for designing antibacterial drugs. Here we report the crystal structure of biosynthetic alanine racemase (Alr) from a pathogenic bacteria Pseudomonas aeruginosa PAO1. Structural studies showed that P. aeruginosa Alr (PaAlr) adopts a conserved homodimer structure. A guest substrate d-lysine was observed in the active site and refined to dual-conformation. Two buffer ions, malonate and acetate, were bound in the proximity to d-lysine. Biochemical characterization revealed the optimal reaction conditions for PaAlr.

PubMed: 29964014
DOI: 10.1016/j.bbrc.2018.06.155

Experimental method

X-RAY DIFFRACTION (2.5 Å)