2f00: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2f00.jpg|left|200px]]
{{Seed}}
[[Image:2f00.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2f00|  PDB=2f00  |  SCENE=  }}  
{{STRUCTURE_2f00|  PDB=2f00  |  SCENE=  }}  


'''Escherichia coli MurC'''
===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.
The line below this paragraph, {{ABSTRACT_PUBMED_17139082}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17139082 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_17139082}}


==About this Structure==
==About this Structure==
Line 20: Line 24:
==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/17139082 17139082]
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:[http://www.ncbi.nlm.nih.gov/pubmed/17139082 17139082]
Purification, crystallization and preliminary X-ray analysis of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC)., Deva T, Pryor KD, Leiting B, Baker EN, Smith CA, Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1510-3. Epub 2003, Jul 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12876369 12876369]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 30: Line 36:
[[Category: Atpase]]
[[Category: Atpase]]
[[Category: Bacterial cell wall]]
[[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 Tue Jul 29 08:21:15 2008''
Retrieved from "https://proteopedia.org/2f00"