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TitleSynthesis and characterization of the arylomycin lipoglycopeptide antibiotics and the crystallographic analysis of their complex with signal peptidase.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 133, Page 17869-17877, Year 2011
Publish dateMay 13, 2011 (structure data deposition date)
AuthorsLiu, J. / Luo, C. / Smith, P.A. / Chin, J.K. / Page, M.G. / Paetzel, M. / Romesberg, F.E.
External linksJ. Am. Chem. Soc. / PubMed:21999324
MethodsX-ray diffraction
Resolution2.44 Å
Structure data

PDB-3s04:
Crystal structure of Escherichia coli type I signal peptidase in complex with an Arylomycin Lipoglycopeptide Antibiotic
Method: X-RAY DIFFRACTION / Resolution: 2.44 Å

Chemicals

ChemComp-02U:
14-methylhexadec-9-enoic acid

ChemComp-RAM:
alpha-L-rhamnopyranose

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
  • streptomyces sp. (bacteria)
KeywordsHYDROLASE/ANTIBIOTIC / mostly-beta fold / Membrane bound / serine protease / Secreted preproteins / Cytoplasmic membrane / HYDROLASE-ANTIBIOTIC complex / signal peptidase / leader peptidase / signal peptide / leader peptide / serine-lysine dyad

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