« Previous Abstract"Soil nutrient effects on oviposition preference, larval performance, and chemical defense of a specialist insect herbivore"    Next Abstract"Polyommatus ripartii: the biological basis for the conservation and the morphology of the developmental stages of a critically endangered, relict population in central Europe" »

Science

Title:		Structure of the integral membrane protein CAAX protease Ste24p
Author(s):		Pryor EE; Horanyi PS; Clark KM; Fedoriw N; Connelly SM; Koszelak-Rosenblum M; Zhu G; Malkowski MG; Wiener MC; Dumont ME;
Address:		"Membrane Protein Structural Biology Consortium, USA"
Journal Title:		Science
Year:		2013
Volume:		339
Issue:		6127
Page Number:		1600 - 1604
DOI:		10.1126/science.1232048
ISSN/ISBN:		1095-9203 (Electronic) 0036-8075 (Print) 0036-8075 (Linking)
Abstract:		"Posttranslational lipidation provides critical modulation of the functions of some proteins. Isoprenoids (i.e., farnesyl or geranylgeranyl groups) are attached to cysteine residues in proteins containing C-terminal CAAX sequence motifs (where A is an aliphatic residue and X is any residue). Isoprenylation is followed by cleavage of the AAX amino acid residues and, in some cases, by additional proteolytic cuts. We determined the crystal structure of the CAAX protease Ste24p, a zinc metalloprotease catalyzing two proteolytic steps in the maturation of yeast mating pheromone a-factor. The Ste24p core structure is a ring of seven transmembrane helices enclosing a voluminous cavity containing the active site and substrate-binding groove. The cavity is accessible to the external milieu by means of gaps between splayed transmembrane helices. We hypothesize that cleavage proceeds by means of a processive mechanism of substrate insertion, translocation, and ejection"
Keywords:		"Amino Acid Sequence Catalytic Domain Cell Membrane/*enzymology Crystallography, X-Ray Membrane Proteins/*chemistry Metalloendopeptidases/*chemistry Molecular Sequence Data Protein Structure, Secondary Saccharomyces cerevisiae Proteins/*chemistry Substrate;"
Notes:		"MedlinePryor, Edward E Jr Horanyi, Peter S Clark, Kathleen M Fedoriw, Nadia Connelly, Sara M Koszelak-Rosenblum, Mary Zhu, Guangyu Malkowski, Michael G Wiener, Michael C Dumont, Mark E eng P30 CA044579/CA/NCI NIH HHS/ U54 GM094611/GM/NIGMS NIH HHS/ Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S. 2013/03/30 Science. 2013 Mar 29; 339(6127):1600-4. doi: 10.1126/science.1232048"