Source:http://linkedlifedata.com/resource/pubmed/id/10972821
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
2000-11-15
|
| pubmed:abstractText |
The class B M1-V577 penicillin-binding protein (PBP) 3 of Escherichia coli consists of a M1-L39 membrane anchor (bearing a cytosolic tail) that is linked via a G40-S70 intervening peptide to an R71-I236 non-catalytic module (containing the conserved motifs 1-3) itself linked via motif 4 to a D237-V577 catalytic module (containing the conserved motifs 5-7 of the penicilloyl serine transferases superfamily). It has been proposed that during cell septation the peptidoglycan crosslinking activity of the acyl transferase module of PBP3 is regulated by the associated M1-I236 polypeptide itself in interaction with other components of the divisome. The fold adopted by the R71-V577 polypeptide of PBP3 has been modelled by reference to the corresponding R76-S634 polypeptide of the class B Streptococcus pneumoniae PBP2x. Based on these data and the results of site-directed mutagenesis of motifs 1-3 and of peptide segments of high amphiphilicity (identified from hydrophobic moment plots), the M1-I236 polypeptide of PBP3 appears to be precisely designed to work in the way proposed. The membrane anchor and the G40-S70 sequence (containing the G57-Q66 peptide segment) upstream from the non-catalytic module have the information ensuring that PBP3 undergoes proper insertion within the divisome at the cell septation site. Motif 1 and the I74-L82 overlapping peptide segment, motif 2 and the H160-G172 overlapping peptide segment, and the G188-D197 motif 3 are located at or close to the intermodule junction. They contain the information ensuring that PBP3 folds correctly and the acyl transferase catalytic centre adopts the active configuration. The E206-V217 peptide segment is exposed at the surface of the non-catalytic module. It has the information ensuring that PBP3 fulfils its cell septation activity within the fully complemented divisome.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/FtsI protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Hexosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Muramoylpentapeptide...,
http://linkedlifedata.com/resource/pubmed/chemical/Penicillin-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptidoglycan Glycosyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Peptidyl Transferases
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0950-382X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
37
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1019-31
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:10972821-Amino Acid Motifs,
pubmed-meshheading:10972821-Amino Acid Sequence,
pubmed-meshheading:10972821-Bacterial Proteins,
pubmed-meshheading:10972821-Binding Sites,
pubmed-meshheading:10972821-Carrier Proteins,
pubmed-meshheading:10972821-Escherichia coli,
pubmed-meshheading:10972821-Escherichia coli Proteins,
pubmed-meshheading:10972821-Hexosyltransferases,
pubmed-meshheading:10972821-Molecular Sequence Data,
pubmed-meshheading:10972821-Multienzyme Complexes,
pubmed-meshheading:10972821-Muramoylpentapeptide Carboxypeptidase,
pubmed-meshheading:10972821-Penicillin-Binding Proteins,
pubmed-meshheading:10972821-Peptides,
pubmed-meshheading:10972821-Peptidoglycan Glycosyltransferase,
pubmed-meshheading:10972821-Peptidyl Transferases,
pubmed-meshheading:10972821-Structure-Activity Relationship
|
| pubmed:year |
2000
|
| pubmed:articleTitle |
Differential functionalities of amphiphilic peptide segments of the cell-septation penicillin-binding protein 3 of Escherichia coli.
|
| pubmed:affiliation |
Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie, B6, Sart Tilman, B-4000 Liège, Belgium. mng.disteche@ulg.ac.be
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|