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J Biol Chem. 2013 May 31;288(22):15430-6. doi: 10.1074/jbc.R112.422378. Epub 2013 Apr 12.

Structure and mechanism of rhomboid protease.

Author information

1
Department of Pharmacology, Yale School of Medicine, New Haven, Connecticut 06520, USA. ya.ha@yale.edu

Abstract

Rhomboid protease was first discovered in Drosophila. Mutation of the fly gene interfered with growth factor signaling and produced a characteristic phenotype of a pointed head skeleton. The name rhomboid has since been widely used to describe a large family of related membrane proteins that have diverse biological functions but share a common catalytic core domain composed of six membrane-spanning segments. Most rhomboid proteases cleave membrane protein substrates near the N terminus of their transmembrane domains. How these proteases function within the confines of the membrane is not completely understood. Recent progress in crystallographic analysis of the Escherichia coli rhomboid protease GlpG in complex with inhibitors has provided new insights into the catalytic mechanism of the protease and its conformational change. Improved biochemical assays have also identified a substrate sequence motif that is specifically recognized by many rhomboid proteases.

KEYWORDS:

Enzyme Mechanisms; Membrane Proteins; Protein Structure; Rhomboid Protease; Serine Protease

PMID:
23585569
PMCID:
PMC3668704
DOI:
10.1074/jbc.R112.422378
[Indexed for MEDLINE]
Free PMC Article

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