Three-dimensional structure of tetrahydrodipicolinate N- succinyltransferase

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

Research output: Contribution to journalArticle

62 Citations (Scopus)

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
StatePublished - Jan 21 1997

Fingerprint

R388
Amino Acid Motifs
Peptidoglycan
Coenzyme A
Cobalt
Lysine
Catalytic Domain
Bacteria
Crystal structure
Binding Sites
X-Rays
Ions
Amino Acids
X rays
Enzymes
benzenesulfonic acid
succinyl-coenzyme A
succinyl-CoA-tetrahydrodipicolinate N-succinyltransferase

ASJC Scopus subject areas

  • Biochemistry

Cite this

Three-dimensional structure of tetrahydrodipicolinate N- succinyltransferase. / Beaman, Todd W.; Binder, David A.; Blanchard, John S.; Roderick, Steven L.

In: Biochemistry, Vol. 36, No. 3, 21.01.1997, p. 489-494.

Research output: Contribution to journalArticle

Beaman, Todd W. ; Binder, David A. ; Blanchard, John S. ; Roderick, Steven L. / Three-dimensional structure of tetrahydrodipicolinate N- succinyltransferase. In: Biochemistry. 1997 ; Vol. 36, No. 3. pp. 489-494.
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AB - 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.

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