3S04

Crystal structure of Escherichia coli type I signal peptidase in complex with an Arylomycin Lipoglycopeptide Antibiotic

Summary for 3S04

Entry DOI	10.2210/pdb3s04/pdb
Related	1B12 1KN9 1T7D 3IIQ
Related PRD ID	PRD_000813
Descriptor	Signal peptidase I, Glyco-Arylomycin, 14-methylhexadec-9-enoic acid, ... (5 entities in total)
Functional Keywords	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, hydrolase/antibiotic
Biological source	Escherichia coli More
Cellular location	Cell inner membrane; Multi-pass membrane protein: P00803
Total number of polymer chains	4
Total formula weight	58346.16
Authors	Paetzel, M.,Luo, C. (deposition date: 2011-05-13, release date: 2011-10-05, Last modification date: 2023-12-06)
Primary citation	Liu, J.,Luo, C.,Smith, P.A.,Chin, J.K.,Page, M.G.,Paetzel, M.,Romesberg, F.E. Synthesis and characterization of the arylomycin lipoglycopeptide antibiotics and the crystallographic analysis of their complex with signal peptidase. J.Am.Chem.Soc., 133:17869-17877, 2011 Cited by PubMed: 21999324 DOI: 10.1021/ja207318n PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.44 Å)

Structure validation