2f00
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2f00.jpg|left|200px]] | [[Image:2f00.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2f00", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_2f00| PDB=2f00 | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Escherichia coli MurC''' | '''Escherichia coli MurC''' | ||
| Line 30: | Line 27: | ||
[[Category: Smith, C A.]] | [[Category: Smith, C A.]] | ||
[[Category: Squire, C J.]] | [[Category: Squire, C J.]] | ||
| - | [[Category: | + | [[Category: Amide bond ligase]] |
| - | [[Category: | + | [[Category: Atpase]] |
| - | [[Category: | + | [[Category: Bacterial cell wall]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:18:06 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:18, 4 May 2008
Escherichia coli MurC
Overview
The bacterial cell wall provides essential protection from the external environment and confers strength and rigidity to counteract internal osmotic pressure. Without this layer the cell would be easily ruptured and it is for this reason that biosynthetic pathways leading to the formation of peptidoglycan have for many years been a prime target for effective antibiotics. Central to this pathway are four similar ligase enzymes which add peptide groups to glycan moieties. As part of a program to better understand the structure-function relationships in these four enzymes, the crystal structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC) has been determined to 2.6 A resolution. The structure was solved by multiwavelength anomalous diffraction methods from a single selenomethionine-substituted crystal and refined to a crystallographic R factor of 0.212 (R(free) = 0.259). The enzyme has a modular multi-domain structure very similar to those of other members of the mur family of ATP-dependent amide-bond ligases. Detailed comparison of these four enzymes shows that considerable conformational changes are possible. These changes, together with the recruitment of two different N-terminal domains, allow this family of enzymes to bind a substrate which is identical at one end and at the other has the growing peptide tail which will ultimately become part of the rigid bacterial cell wall. Comparison of the E. coli and Haemophilus influenzae structures and analysis of the sequences of known MurC enzymes indicate the presence of a ;dimerization' motif in almost 50% of the MurC enzymes and points to a highly conserved loop in domain 3 that may play a key role in amino-acid ligand specificity.
About this Structure
2F00 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC)., Deva T, Baker EN, Squire CJ, Smith CA, Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1466-74. Epub 2006, Nov 23. PMID:17139082 Page seeded by OCA on Sun May 4 03:18:06 2008
