| Literature DB >> 26370567 |
Yue Fu1, Kevin E Bruce2, Britta Rued2, Malcolm E Winkler2, David P Giedroc3.
Abstract
FtsX is an integral membrane protein from Streptococcus pneumoniae (pneumococcus) that harbors an extracellular loop 1 domain (FtsX(Spn)ECL1) that interacts with PcsB, an peptidoglycan hydrolase that is essential for cell growth and division. Here, we report nearly complete backbone and side chain resonance assignments and a secondary structural analysis of FtsX(Spn)ECL1 (residues 47-168 of FtsX) as first steps toward structure determination of FtsX(Spn)ECL1.Entities:
Keywords: ABC transporter; Allostery; Bacterial cell wall; Divisome; Extracellular signaling; Peptidoglycan hydrolysis
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Year: 2015 PMID: 26370567 PMCID: PMC4789122 DOI: 10.1007/s12104-015-9644-9
Source DB: PubMed Journal: Biomol NMR Assign ISSN: 1874-270X Impact factor: 0.746