3bxy is a 1 chain structure with sequence from Escherichia coli o157:h7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Tetrahydrodipicolinate N-succinyltransferase is an enzyme present in many bacteria that catalyzes the first step of the succinylase pathway for the synthesis of meso-diaminopimelate and the amino acid L-lysine. Inhibition of the synthesis of meso-diaminopimelate, a component of peptidoglycan present in the cell wall of bacteria, is a potential route for the development of novel anti-bacterial agents. Here, we report the crystal structure of the DapD tetrahydrodipicolinate N-succinyltransferase from Escherichia coli at 2.0 A resolution. Comparison of the structure with the homologous enzyme from Mycobacterium bovis reveals the C-terminal helix undergoes a large rearrangement upon substrate binding, which contributes to cooperativity in substrate binding.
Structure of Escherichia coli tetrahydrodipicolinate N-succinyltransferase reveals the role of a conserved C-terminal helix in cooperative substrate binding.,Nguyen L, Kozlov G, Gehring K FEBS Lett. 2008 Mar 5;582(5):623-6. Epub 2008 Jan 31. PMID:18242192[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑Nguyen L, Kozlov G, Gehring K. Structure of Escherichia coli tetrahydrodipicolinate N-succinyltransferase reveals the role of a conserved C-terminal helix in cooperative substrate binding. FEBS Lett. 2008 Mar 5;582(5):623-6. Epub 2008 Jan 31. PMID:18242192 doi:10.1016/j.febslet.2008.01.032
