1e8c: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1e8c.gif|left|200px]]
{{Seed}}
[[Image:1e8c.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1e8c|  PDB=1e8c  |  SCENE=  }}  
{{STRUCTURE_1e8c|  PDB=1e8c  |  SCENE=  }}  


'''STRUCTURE OF MURE THE UDP-N-ACETYLMURAMYL TRIPEPTIDE SYNTHETASE FROM E. COLI'''
===STRUCTURE OF MURE THE UDP-N-ACETYLMURAMYL TRIPEPTIDE SYNTHETASE FROM E. COLI===




==Overview==
<!--  
UDP-N-acetylmuramoyl-l-alanyl-d-glutamate:meso-diaminopimelate ligase is a cytoplasmic enzyme that catalyzes the addition of meso-diaminopimelic acid to nucleotide precursor UDP-N-acetylmuramoyl-l-alanyl-d-glutamate in the biosynthesis of bacterial cell-wall peptidoglycan. The crystal structure of the Escherichia coli enzyme in the presence of the final product of the enzymatic reaction, UDP-MurNAc-l-Ala-gamma-d-Glu-meso-A(2)pm, has been solved to 2.0 A resolution. Phase information was obtained by multiwavelength anomalous dispersion using the K shell edge of selenium. The protein consists of three domains, two of which have a topology reminiscent of the equivalent domain found in the already established three-dimensional structure of the UDP-N-acetylmuramoyl-l-alanine: D-glutamate-ligase (MurD) ligase, which catalyzes the immediate previous step of incorporation of d-glutamic acid in the biosynthesis of the peptidoglycan precursor. The refined model reveals the binding site for UDP-MurNAc-l-Ala-gamma-d-Glu-meso-A(2)pm, and comparison with the six known MurD structures allowed the identification of residues involved in the enzymatic mechanism. Interestingly, during refinement, an excess of electron density was observed, leading to the conclusion that, as in MurD, a carbamylated lysine residue is present in the active site. In addition, the structural determinant responsible for the selection of the amino acid to be added to the nucleotide precursor was identified.
The line below this paragraph, {{ABSTRACT_PUBMED_11124264}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11124264 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_11124264}}


==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Ligase]]
[[Category: Ligase]]
[[Category: Peptidoglycan biosynthesis]]
[[Category: Peptidoglycan biosynthesis]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:47:20 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:18:48 2008''

Revision as of 21:18, 30 June 2008

File:1e8c.png

Template:STRUCTURE 1e8c

STRUCTURE OF MURE THE UDP-N-ACETYLMURAMYL TRIPEPTIDE SYNTHETASE FROM E. COLI

Template:ABSTRACT PUBMED 11124264

About this Structure

1E8C is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of UDP-N-acetylmuramoyl-L-alanyl-D-glutamate: meso-diaminopimelate ligase from Escherichia coli., Gordon E, Flouret B, Chantalat L, van Heijenoort J, Mengin-Lecreulx D, Dideberg O, J Biol Chem. 2001 Apr 6;276(14):10999-1006. Epub 2000 Dec 20. PMID:11124264

Page seeded by OCA on Tue Jul 1 00:18:48 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1e8c&oldid=591087"