3stj
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Crystal structure of the protease + PDZ1 domain of DegQ from Escherichia coli
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Structural highlights
FunctionDEGQ_ECOLI DegQ could degrade transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. DegQ is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for a beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable to be cleaved, thereby preventing non-specific proteolysis of folded proteins. DegQ can substitute for the periplasmic protease DegP.[1] [2] References
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This page was last modified 09:56, 1 March 2024.