Summary for 4QHR
| Entry DOI | 10.2210/pdb4qhr/pdb |
| Descriptor | Alanine racemase (2 entities in total) |
| Functional Keywords | alpha/beta barrel, racemization, isomerase |
| Biological source | Acinetobacter baumannii |
| Total number of polymer chains | 2 |
| Total formula weight | 79733.12 |
| Authors | Davis, E.,Scaletti-Hutchinson, E.,Nakatani, Y.,Krause, K.L. (deposition date: 2014-05-29, release date: 2015-05-06, Last modification date: 2025-03-26) |
| Primary citation | Davis, E.,Scaletti-Hutchinson, E.,Opel-Reading, H.,Nakatani, Y.,Krause, K.L. The structure of alanine racemase from Acinetobacter baumannii ACTA CRYSTALLOGR.,SECT.F, 70:1199-1205, 2014 Cited by PubMed Abstract: Acinetobacter baumannii is an opportunistic Gram-negative bacterium which is a common cause of hospital-acquired infections. Numerous antibiotic-resistant strains exist, emphasizing the need for the development of new antimicrobials. Alanine racemase (Alr) is a pyridoxal 5'-phosphate dependent enzyme that is responsible for racemization between enantiomers of alanine. As D-alanine is an essential component of the bacterial cell wall, its inhibition is lethal to prokaryotes, making it an excellent antibiotic drug target. The crystal structure of A. baumannii alanine racemase (AlrAba) from the highly antibiotic-resistant NCTC13302 strain has been solved to 1.9 Å resolution. Comparison of AlrAba with alanine racemases from closely related bacteria demonstrates a conserved overall fold. The substrate entryway and active site of the enzymes were shown to be highly conserved. The structure of AlrAba will provide the template required for future structure-based drug-design studies. PubMed: 25195891DOI: 10.1107/S2053230X14017725 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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