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Template:STRUCTURE 3lgu

Contents 1 Y162A mutant of the DegS-deltaPDZ protease 2 Function 3 About this Structure 4 Reference

Y162A mutant of the DegS-deltaPDZ protease

Template:ABSTRACT PUBMED 20739286

Function

[DEGS_ECOLI] When heat shock or other environmental stresses disrupt protein folding in the periplasm, DegS senses the accumulation of unassembled outer membrane porins (OMPs) and then initiates RseA (anti sigma-E factor) degradation by cleaving it in its periplasmic domain, making it an attractive substrate for subsequent cleavage by RseP. This cascade that ultimately leads to the sigma-E-driven expression of a variety of factors dealing with folding stress in the periplasm and OMP assembly.^{[1] [2]}

About this Structure

3lgu is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

• Sohn J, Grant RA, Sauer RT. Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution. J Biol Chem. 2010 Oct 29;285(44):34039-47. Epub 2010 Aug 24. PMID:20739286 doi:10.1074/jbc.M110.135541

1. ↑ Alba BM, Leeds JA, Onufryk C, Lu CZ, Gross CA. DegS and YaeL participate sequentially in the cleavage of RseA to activate the sigma(E)-dependent extracytoplasmic stress response. Genes Dev. 2002 Aug 15;16(16):2156-68. PMID:12183369 doi:10.1101/gad.1008902
2. ↑ Meltzer M, Hasenbein S, Mamant N, Merdanovic M, Poepsel S, Hauske P, Kaiser M, Huber R, Krojer T, Clausen T, Ehrmann M. Structure, function and regulation of the conserved serine proteases DegP and DegS of Escherichia coli. Res Microbiol. 2009 Nov;160(9):660-6. doi: 10.1016/j.resmic.2009.07.012. Epub, 2009 Aug 18. PMID:19695325 doi:10.1016/j.resmic.2009.07.012