3tdt: Difference between revisions
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'''COMPLEX OF TETRAHYDRODIPICOLINATE N-SUCCINYLTRANSFERASE WITH 2-AMINO-6-OXOPIMELATE AND COENZYME A''' | {{Structure | ||
|PDB= 3tdt |SIZE=350|CAPTION= <scene name='initialview01'>3tdt</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene> and <scene name='pdbligand=26P:2-AMINO-6-OXOPIMELIC ACID'>26P</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/2,3,4,5-tetrahydropyridine-2,6-dicarboxylate_N-succinyltransferase 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.117 2.3.1.117] | |||
|GENE= DAPD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1765 Mycobacterium bovis]) | |||
}} | |||
'''COMPLEX OF TETRAHYDRODIPICOLINATE N-SUCCINYLTRANSFERASE WITH 2-AMINO-6-OXOPIMELATE AND COENZYME A''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
3TDT is a [ | 3TDT 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=3TDT OCA]. | ||
==Reference== | ==Reference== | ||
The conformational change and active site structure of tetrahydrodipicolinate N-succinyltransferase., Beaman TW, Blanchard JS, Roderick SL, Biochemistry. 1998 Jul 21;37(29):10363-9. PMID:[http:// | The conformational change and active site structure of tetrahydrodipicolinate N-succinyltransferase., Beaman TW, Blanchard JS, Roderick SL, Biochemistry. 1998 Jul 21;37(29):10363-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9671504 9671504] | ||
[[Category: 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase]] | [[Category: 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase]] | ||
[[Category: Mycobacterium bovis]] | [[Category: Mycobacterium bovis]] | ||
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[[Category: lysine biosynthesis]] | [[Category: lysine biosynthesis]] | ||
''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 19:07:19 2008'' | ||
Revision as of 20:07, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | and | ||||||
| Gene: | DAPD (Mycobacterium bovis) | ||||||
| Activity: | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase, with EC number 2.3.1.117 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
COMPLEX OF TETRAHYDRODIPICOLINATE N-SUCCINYLTRANSFERASE WITH 2-AMINO-6-OXOPIMELATE AND COENZYME A
OverviewOverview
Tetrahydrodipicolinate (THDP) N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to L-2-(succinylamino)-6-oxopimelate and CoA. This reaction represents the committed step of the succinylase branch of the diaminopimelate/L-lysine biosynthetic pathway by which many bacteria synthesize meso-diaminopimelate, a component of peptidoglycan, and L-lysine from L-aspartate. The crystal structures of THDP succinyltransferase in complex with the substrate/cofactor pairs L-2-aminopimelate/coenzyme A and L-2-amino-6-oxopimelate/coenzyme A have been determined and refined to 2.0 A resolution. The active site of the enzyme is a long narrow groove located at the interface between two left-handed parallel beta-helix (LbetaH) structural domains of the trimeric enzyme. On binding the amino acid acceptor and cofactor, this groove is covered by residues from the C-terminus of one subunit and a flexible loop excluded from the LbetaH domain of an adjacent subunit to form a tunnel. This conformational change is directly related to interactions between the enzyme and the bound amino acid substrate and cofactor and serves to shield the ligands from bulk solvent and to orient the nucleophilic amino group of the amino acid acceptor toward the mercaptoethylamine group of the cofactor.
About this StructureAbout this Structure
3TDT is a Single protein structure of sequence from Mycobacterium bovis. Full crystallographic information is available from OCA.
ReferenceReference
The conformational change and active site structure of tetrahydrodipicolinate N-succinyltransferase., Beaman TW, Blanchard JS, Roderick SL, Biochemistry. 1998 Jul 21;37(29):10363-9. PMID:9671504
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