2jfg: Difference between revisions

Revision as of 14:31, 29 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:2jfg.png

Template:STRUCTURE 2jfg

CRYSTAL STRUCTURE OF MURD LIGASE IN COMPLEX WITH UMA AND ADPCRYSTAL STRUCTURE OF MURD LIGASE IN COMPLEX WITH UMA AND ADP

Template:ABSTRACT PUBMED 17507028

About this StructureAbout this Structure

2JFG is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structural and functional characterization of enantiomeric glutamic acid derivatives as potential transition state analogue inhibitors of MurD ligase., Kotnik M, Humljan J, Contreras-Martel C, Oblak M, Kristan K, Herve M, Blanot D, Urleb U, Gobec S, Dessen A, Solmajer T, J Mol Biol. 2007 Jun 29;370(1):107-15. Epub 2007 May 4. PMID:17507028

Page seeded by OCA on Tue Jul 29 14:31:41 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2jfg.jpg|left|200px]]
+{{Seed}}
+[[Image:2jfg.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2jfg|  PDB=2jfg  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF MURD LIGASE IN COMPLEX WITH UMA AND ADP'''
+===CRYSTAL STRUCTURE OF MURD LIGASE IN COMPLEX WITH UMA AND ADP===
-==Overview==
+<!--
-Mur ligases play an essential role in the intracellular biosynthesis of bacterial peptidoglycan, the main component of the bacterial cell wall, and represent attractive targets for the design of novel antibacterials. UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase (MurD) catalyses the addition of D-glutamic acid to the cytoplasmic intermediate UDP-N-acetylmuramoyl-L-alanine (UMA) and is the second in the series of Mur ligases. MurD ligase is highly stereospecific for its substrate, D-glutamic acid (D-Glu). Here, we report the high resolution crystal structures of MurD in complexes with two novel inhibitors designed to mimic the transition state of the reaction, which contain either the D-Glu or the L-Glu moiety. The binding modes of N-sulfonyl-D-Glu and N-sulfonyl-L-Glu derivatives were also characterised kinetically. The results of this study represent an excellent starting point for further development of novel inhibitors of this enzyme.
+The line below this paragraph, {{ABSTRACT_PUBMED_17507028}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17507028 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17507028}}
 ==About this Structure==
@@ Line 45: / Line 49: @@
 [[Category: Peptidoglycan synthesis]]
 [[Category: Uma]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 08:49:53 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:31:41 2008''