3tdt: Difference between revisions

Revision as of 13:08, 3 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3tdt.png

Template:STRUCTURE 3tdt

COMPLEX OF TETRAHYDRODIPICOLINATE N-SUCCINYLTRANSFERASE WITH 2-AMINO-6-OXOPIMELATE AND COENZYME ACOMPLEX OF TETRAHYDRODIPICOLINATE N-SUCCINYLTRANSFERASE WITH 2-AMINO-6-OXOPIMELATE AND COENZYME A

Template:ABSTRACT PUBMED 9671504

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

Page seeded by OCA on Thu Jul 3 13:08:23 2008

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-[[Image:3tdt.jpg|left|200px]]
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 {{STRUCTURE_3tdt|  PDB=3tdt  |  SCENE=  }}
-'''COMPLEX OF TETRAHYDRODIPICOLINATE N-SUCCINYLTRANSFERASE WITH 2-AMINO-6-OXOPIMELATE AND COENZYME A'''
+===COMPLEX OF TETRAHYDRODIPICOLINATE N-SUCCINYLTRANSFERASE WITH 2-AMINO-6-OXOPIMELATE AND COENZYME A===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9671504}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9671504 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9671504}}
 ==About this Structure==
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 [[Category: Acyltransferase]]
 [[Category: Lysine biosynthesis]]
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