1tdt: Difference between revisions
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tdt OCA], [http://www.ebi.ac.uk/pdbsum/1tdt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tdt RCSB]</span> | |||
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:54:41 2008'' | ||
Revision as of 23:54, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THREE-DIMENSIONAL STRUCTURE OF TETRAHYDRODIPICOLINATE-N-SUCCINLYTRANSFERASE
OverviewOverview
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 StructureAbout this Structure
1TDT is a Single protein structure of sequence from Mycobacterium bovis. Full crystallographic information is available from OCA.
ReferenceReference
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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