3tdt: Difference between revisions

New page: left|200px<br /><applet load="3tdt" size="450" color="white" frame="true" align="right" spinBox="true" caption="3tdt, resolution 2.0Å" /> '''COMPLEX OF TETRAHYDRO...
 
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[[Image:3tdt.jpg|left|200px]]<br /><applet load="3tdt" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:3tdt.jpg|left|200px]]<br /><applet load="3tdt" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="3tdt, resolution 2.0&Aring;" />
caption="3tdt, resolution 2.0&Aring;" />
'''COMPLEX OF TETRAHYDRODIPICOLINATE N-SUCCINYLTRANSFERASE WITH 2-AMINO-6-OXOPIMELATE AND COENZYME A'''<br />
'''COMPLEX OF TETRAHYDRODIPICOLINATE N-SUCCINYLTRANSFERASE WITH 2-AMINO-6-OXOPIMELATE AND COENZYME A'''<br />


==Overview==
==Overview==
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.
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 Structure==
==About this Structure==
3TDT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_bovis Mycobacterium bovis] with COA and 26P as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3TDT OCA].  
3TDT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_bovis Mycobacterium bovis] with <scene name='pdbligand=COA:'>COA</scene> and <scene name='pdbligand=26P:'>26P</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TDT OCA].  


==Reference==
==Reference==
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[[Category: Mycobacterium bovis]]
[[Category: Mycobacterium bovis]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Beaman, T.W.]]
[[Category: Beaman, T W.]]
[[Category: Blanchard, J.S.]]
[[Category: Blanchard, J S.]]
[[Category: Roderick, S.L.]]
[[Category: Roderick, S L.]]
[[Category: 26P]]
[[Category: 26P]]
[[Category: COA]]
[[Category: COA]]
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[[Category: lysine biosynthesis]]
[[Category: lysine biosynthesis]]


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