4XKY

Structure of dihydrodipicolinate synthase from the commensal bacterium Bacteroides thetaiotaomicron at 2.1 A resolution

Summary for 4XKY

• Entry DOI: 10.2210/pdb4xky/pdb
• Descriptor: Dihydrodipicolinate synthase, ACETATE ION, SODIUM ION, ... (5 entities in total)
• Functional Keywords: dihydrodipicolinate synthase, diaminopimelate, lysine, tetramer, aldolase, lyase
• Biological source: Bacteroides thetaiotaomicron; More
• Total number of polymer chains: 4
• Total formula weight: 131309.60

Authors

Mank, N.J.,Arnette, A.K.,Klapper, V.G.,Chruszcz, M. (deposition date: 2015-01-12, release date: 2015-04-01, Last modification date: 2024-11-20)

Primary citation

Mank, N.,Arnette, A.,Klapper, V.,Offermann, L.,Chruszcz, M.
Structure of dihydrodipicolinate synthase from the commensal bacterium Bacteroides thetaiotaomicron at 2.1 angstrom resolution.
Acta Crystallogr.,Sect.F, 71:449-454, 2015

PubMed Abstract: Dihydrodipicolinate synthase (DapA) catalyzes the first committed step of the diaminopimelate biosynthetic pathway of lysine. It has been shown to be an essential enzyme in many bacteria and has been the subject of research to generate novel antibiotics. However, this pathway is present in both pathogenic and commensal bacteria, and antibiotics targeting DapA may interfere with normal gut colonization. Bacteroides thetaiotaomicron is a Gram-negative commensal bacterium that makes up a large proportion of the normal microbiota of the human gut. The structure of DapA from B. thetaiotaomicron (BtDapA) has been determined. This structure will help to guide the generation of selectively active antibiotic compounds targeting DapA.

PubMed: 25849508
DOI: 10.1107/S2053230X15004628

Experimental method

X-RAY DIFFRACTION (2.1 Å)