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| - | [[Image:1xp4.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1xp4| PDB=1xp4 | SCENE= }} | | {{STRUCTURE_1xp4| PDB=1xp4 | SCENE= }} |
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| - | '''Crystal structure of a peptidoglycan synthesis regulatory factor (PBP3) from Streptococcus pneumoniae'''
| + | ===Crystal structure of a peptidoglycan synthesis regulatory factor (PBP3) from Streptococcus pneumoniae=== |
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| - | ==Overview==
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| - | 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. |
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| | + | {{ABSTRACT_PUBMED_15596446}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[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
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
