1xp4: 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:1xp4.jpg|left|200px]]
{{Seed}}
[[Image:1xp4.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1xp4|  PDB=1xp4  |  SCENE=  }}  
{{STRUCTURE_1xp4|  PDB=1xp4  |  SCENE=  }}  


'''Crystal structure of a peptidoglycan synthesis regulatory factor (PBP3) from Streptococcus pneumoniae'''
===Crystal structure of a peptidoglycan synthesis regulatory factor (PBP3) from Streptococcus pneumoniae===




==Overview==
<!--  
Penicillin-binding proteins (PBPs) are membrane-associated enzymes which perform critical functions in the bacterial cell division process. The single d-Ala,d-Ala (d,d)-carboxypeptidase in Streptococcus pneumoniae, PBP3, has been shown to play a key role in control of availability of the peptidoglycal substrate during cell growth. Here, we have biochemically characterized and solved the crystal structure of a soluble form of PBP3 to 2.8 A resolution. PBP3 folds into an NH(2)-terminal, d,d-carboxypeptidase-like domain, and a COOH-terminal, elongated beta-rich region. The carboxypeptidase domain harbors the classic signature of the penicilloyl serine transferase superfamily, in that it contains a central, five-stranded antiparallel beta-sheet surrounded by alpha-helices. As in other carboxypeptidases, which are present in species whose peptidoglycan stem peptide has a lysine residue at the third position, PBP3 has a 14-residue insertion at the level of its omega loop, a feature that distinguishes it from carboxypeptidases from bacteria whose peptidoglycan harbors a diaminopimelate moiety at this position. PBP3 performs substrate acylation in a highly efficient manner (k(cat)/K(m) = 50,500 M(-1) x s(-1)), an event that may be linked to role in control of pneumococcal peptidoglycan reticulation. A model that places PBP3 poised vertically on the bacterial membrane suggests that its COOH-terminal region could act as a pedestal, placing the active site in proximity to the peptidoglycan and allowing the protein to "skid" on the surface of the membrane, trimming pentapeptides during the cell growth and division processes.
The line below this paragraph, {{ABSTRACT_PUBMED_15596446}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15596446 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15596446}}


==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Five-stranded antiparallel beta-sheet]]
[[Category: Five-stranded antiparallel beta-sheet]]
[[Category: Omega-like loop]]
[[Category: Omega-like loop]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 15:19:17 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:36:08 2008''

Revision as of 18:36, 28 July 2008

File:1xp4.png

Template:STRUCTURE 1xp4

Crystal structure of a peptidoglycan synthesis regulatory factor (PBP3) from Streptococcus pneumoniae

Template:ABSTRACT PUBMED 15596446

About this Structure

1XP4 is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.

Reference

Crystal structure of a peptidoglycan synthesis regulatory factor (PBP3) from Streptococcus pneumoniae., Morlot C, Pernot L, Le Gouellec A, Di Guilmi AM, Vernet T, Dideberg O, Dessen A, J Biol Chem. 2005 Apr 22;280(16):15984-91. Epub 2004 Dec 13. PMID:15596446

Page seeded by OCA on Mon Jul 28 21:36:08 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1xp4&oldid=716500"