3S46

The crystal structure of alanine racemase from streptococcus pneumoniae

Replaces:  3MUB

Summary for 3S46

• Entry DOI: 10.2210/pdb3s46/pdb
• Descriptor: Alanine racemase, BENZOIC ACID (3 entities in total)
• Functional Keywords: alpha/beta barrel, extended beta-strand domain, pyridoxal phosphate cofactor, alanine racemase, carbamylated lysine, isomerase
• Biological source: Streptococcus pneumoniae
• Total number of polymer chains: 2
• Total formula weight: 80455.30

Authors

Im, H.,Sharpe, M.L.,Strych, U.,Davlieva, M.,Krause, K.L. (deposition date: 2011-05-18, release date: 2011-06-22, Last modification date: 2023-12-06)

Primary citation

Im, H.,Sharpe, M.L.,Strych, U.,Davlieva, M.,Krause, K.L.
The crystal structure of alanine racemase from Streptococcus pneumoniae, a target for structure-based drug design.
BMC MICROBIOL., 11:116-116, 2011

PubMed Abstract: Streptococcus pneumoniae is a globally important pathogen. The Gram-positive diplococcus is a leading cause of pneumonia, otitis media, bacteremia, and meningitis, and antibiotic resistant strains have become increasingly common over recent years. Alanine racemase is a ubiquitous enzyme among bacteria and provides the essential cell wall precursor, D-alanine. Since it is absent in humans, this enzyme is an attractive target for the development of drugs against S. pneumoniae and other bacterial pathogens.

PubMed: 21612658
DOI: 10.1186/1471-2180-11-116

Experimental method

X-RAY DIFFRACTION (2 Å)