1kgq: Difference between revisions

Revision as of 10:19, 2 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:1kgq.png

Template:STRUCTURE 1kgq

Crystal Structure of Tetrahydrodipicolinate N-Succinyltransferase in Complex with L-2-aminopimelate and Succinamide-CoACrystal Structure of Tetrahydrodipicolinate N-Succinyltransferase in Complex with L-2-aminopimelate and Succinamide-CoA

Template:ABSTRACT PUBMED 11910040

About this StructureAbout this Structure

1KGQ is a Single protein structure of sequence from Mycobacterium bovis. Full crystallographic information is available from OCA.

ReferenceReference

Acyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferase., Beaman TW, Vogel KW, Drueckhammer DG, Blanchard JS, Roderick SL, Protein Sci. 2002 Apr;11(4):974-9. PMID:11910040

Page seeded by OCA on Wed Jul 2 10:19:20 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1kgq.gif|left|200px]]
+{{Seed}}
+[[Image:1kgq.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1kgq|  PDB=1kgq  |  SCENE=  }}
-'''Crystal Structure of Tetrahydrodipicolinate N-Succinyltransferase in Complex with L-2-aminopimelate and Succinamide-CoA'''
+===Crystal Structure of Tetrahydrodipicolinate N-Succinyltransferase in Complex with L-2-aminopimelate and Succinamide-CoA===
-==Overview==
+<!--
-Tetrahydrodipicolinate N-succinyltransferase (DapD) catalyzes the succinyl-CoA-dependent acylation of L-2-amino-6-oxopimelate to 2-N-succinyl-6-oxopimelate as part of the succinylase branch of the meso-diaminopimelate/lysine biosynthetic pathway of bacteria, blue-green algae, and plants. This pathway provides meso-diaminopimelate as a building block for cell wall peptidoglycan in most bacteria, and is regarded as a target pathway for antibacterial agents. We have solved the X-ray crystal structures of DapD in ternary complexes with pimelate/succinyl-CoA and L-2-aminopimelate with the nonreactive cofactor analog, succinamide-CoA. These structures define the binding conformation of the cofactor succinyl group and its interactions with the enzyme and place its thioester carbonyl carbon in close proximity to the nucleophilic 2-amino group of the acceptor, in support of a direct attack ternary complex mechanism. The acyl group specificity differences between homologous tetrahydrodipicolinate N-acetyl- and N-succinyltransferases can be rationalized with reference to at least three amino acids that interact with or give accessible active site volume to the cofactor succinyl group. These residues account at least in part for the substrate specificity that commits metabolic intermediates to either the succinylase or acetylase branches of the meso-diaminopimelate/lysine biosynthetic pathway.
+The line below this paragraph, {{ABSTRACT_PUBMED_11910040}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11910040 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11910040}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Vogel, K W.]]
 [[Category: Left-handed parallel beta helix]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:43:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 10:19:20 2008''