1JHH

LEXA S119A MUTANT

Summary for 1JHH

• Entry DOI: 10.2210/pdb1jhh/pdb
• Related: 1JHC 1JHE 1JHF
• Descriptor: LEXA REPRESSOR, SULFATE ION (3 entities in total)
• Functional Keywords: lexa sos repressor, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 44841.49

Authors

Luo, Y.,Pfuetzner, R.A.,Mosimann, S.,Little, J.W.,Strynadka, N.C.J. (deposition date: 2001-06-27, release date: 2001-09-19, Last modification date: 2023-08-16)

Primary citation

Luo, Y.,Pfuetzner, R.A.,Mosimann, S.,Paetzel, M.,Frey, E.A.,Cherney, M.,Kim, B.,Little, J.W.,Strynadka, N.C.
Crystal structure of LexA: a conformational switch for regulation of self-cleavage.
Cell(Cambridge,Mass.), 106:585-594, 2001

PubMed Abstract: LexA repressor undergoes a self-cleavage reaction. In vivo, this reaction requires an activated form of RecA, but it occurs spontaneously in vitro at high pH. Accordingly, LexA must both allow self-cleavage and yet prevent this reaction in the absence of a stimulus. We have solved the crystal structures of several mutant forms of LexA. Strikingly, two distinct conformations are observed, one compatible with cleavage, and the other in which the cleavage site is approximately 20 A from the catalytic center. Our analysis provides insight into the structural and energetic features that modulate the interconversion between these two forms and hence the rate of the self-cleavage reaction. We suggest RecA activates the self-cleavage of LexA and related proteins through selective stabilization of the cleavable conformation.

PubMed: 11551506
DOI: 10.1016/S0092-8674(01)00479-2

Experimental method

X-RAY DIFFRACTION (2.1 Å)