1tdt
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(New page: 200px<br /><applet load="1tdt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tdt, resolution 2.2Å" /> '''THREE-DIMENSIONAL STR...)
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Revision as of 01:04, 21 November 2007
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THREE-DIMENSIONAL STRUCTURE OF TETRAHYDRODIPICOLINATE-N-SUCCINLYTRANSFERASE
Overview
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 A, resolution and has been refined to a crystallographic R-factor of 17.0%., The enzyme is trimeric and displays the left-handed parallel beta-helix (L, beta H) structural motif encoded by the "hexapeptide repeat" amino acid, sequence motif [Raetz, C.R.H., & 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 L beta H domain.
About this Structure
1TDT is a Single protein structure of sequence from Mycobacterium bovis. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of tetrahydrodipicolinate N-succinyltransferase., Beaman TW, Binder DA, Blanchard JS, Roderick SL, Biochemistry. 1997 Jan 21;36(3):489-94. PMID:9012664
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