Three-dimensional structure of tetrahydrodipicolinate N- succinyltransferase

Todd W. Beaman, David A. Binder, John S. Blanchard, Steven L. Roderick

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Abstract

The conversion of tetrahydrodipicolinate and succinyl-CoA to N- succinyltetrahydrodipicolinate and CoA is catalyzed by tetrahydrodipicolinate N-succinyltransferase and is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The X-ray crystal structure of THDP succinyltransferase has been determined to 2.2 Å resolution and has been refined to a crystallographic R-factor of 17.0%. The enzyme is trimeric and displays the left-handed parallel β-helix (LβH) structural motif encoded by the 'hexapeptide repeat' amino acid sequence motif [Raetz, C. R. H., and Roderick, S. L. (1995) Science 270, 997-1000]. The approximate location of the active site of THDP succinyltransferase is suggested by the proximity of binding sites for two inhibitors; p-(chloromercuri)benzenesulfonic acid and cobalt ion, both of which bind to the LβH domain.

Original languageEnglish (US)
Pages (from-to)489-494
Number of pages6
JournalBiochemistry
Volume36
Issue number3
DOIs
Publication statusPublished - Jan 21 1997

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ASJC Scopus subject areas

  • Biochemistry

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