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1KN9

CRYSTAL STRUCTURE OF A BACTERIAL SIGNAL PEPTIDASE APO-ENZYME, IMPLICATIONS FOR SIGNAL PEPTIDE BINDING AND THE SER-LYS DYAD MECHANISM.

Summary for 1KN9
Entry DOI10.2210/pdb1kn9/pdb
Related1B12
DescriptorSignal peptidase I (2 entities in total)
Functional Keywordsserine protease, lysine general base, membrane protein, mostly beta-fold, hydrolase
Biological sourceEscherichia coli K12
Cellular locationCell inner membrane ; Multi-pass membrane protein : P00803
Total number of polymer chains4
Total formula weight111866.63
Authors
Paetzel, M.,Dalbey, R.E.,Strynadka, N.C.J. (deposition date: 2001-12-18, release date: 2002-01-30, Last modification date: 2023-08-16)
Primary citationPaetzel, M.,Dalbey, R.E.,Strynadka, N.C.J.
Crystal structure of a bacterial signal peptidase apoenzyme: implications for signal peptide binding and the Ser-Lys dyad mechanism
J.Biol.Chem., 277:9512-9519, 2002
Cited by
PubMed: 11741964
DOI: 10.1074/jbc.M110983200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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