1tdt
From Proteopedia
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- | [[Image:1tdt.gif|left|200px]] | + | [[Image:1tdt.gif|left|200px]] |
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- | '''THREE-DIMENSIONAL STRUCTURE OF TETRAHYDRODIPICOLINATE-N-SUCCINLYTRANSFERASE''' | + | {{Structure |
+ | |PDB= 1tdt |SIZE=350|CAPTION= <scene name='initialview01'>1tdt</scene>, resolution 2.2Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''THREE-DIMENSIONAL STRUCTURE OF TETRAHYDRODIPICOLINATE-N-SUCCINLYTRANSFERASE''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1TDT is a [ | + | 1TDT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_bovis Mycobacterium bovis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TDT OCA]. |
==Reference== | ==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:[http:// | + | Three-dimensional structure of tetrahydrodipicolinate N-succinyltransferase., Beaman TW, Binder DA, Blanchard JS, Roderick SL, Biochemistry. 1997 Jan 21;36(3):489-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9012664 9012664] |
[[Category: Mycobacterium bovis]] | [[Category: Mycobacterium bovis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:17:08 2008'' |
Revision as of 12:17, 20 March 2008
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, resolution 2.2Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
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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