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Biomol NMR Assign. 2016 Apr;10(1):89-92. doi: 10.1007/s12104-015-9644-9. Epub 2015 Sep 14.

1H, 13C, 15N resonance assignments of the extracellular loop 1 domain (ECL1) of Streptococcus pneumoniae D39 FtsX, an essential cell division protein.

Author information

1
Department of Chemistry, Indiana University, 212 S. Hawthorne Drive, Bloomington, IN, 47405-7102, USA.
2
Department of Biology, Indiana University, Bloomington, IN, 47405, USA.
3
Department of Chemistry, Indiana University, 212 S. Hawthorne Drive, Bloomington, IN, 47405-7102, USA. giedroc@indiana.edu.

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.

KEYWORDS:

ABC transporter; Allostery; Bacterial cell wall; Divisome; Extracellular signaling; Peptidoglycan hydrolysis

PMID:
26370567
PMCID:
PMC4789122
DOI:
10.1007/s12104-015-9644-9
[Indexed for MEDLINE]
Free PMC Article

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