4IL3

Crystal Structure of S. mikatae Ste24p

Summary for 4IL3

• Entry DOI: 10.2210/pdb4il3/pdb
• Descriptor: Ste24p, ZINC ION (2 entities in total)
• Functional Keywords: membrane protein, alpha helical, caax protease, a-factor, structural genomics, mpsbc, psi-biology, membrane protein structural biology consortium, hydrolase
• Biological source: Saccharomyces mikatae
• Total number of polymer chains: 2
• Total formula weight: 106810.79

Authors

Pryor Jr., E.E.,Horanyi, P.S.,Clark, K.,Fedoriw, N.,Connelly, S.M.,Koszelak-Rosenblum, M.,Zhu, G.,Malkowski, M.G.,Dumont, M.E.,Wiener, M.C.,Membrane Protein Structural Biology Consortium (MPSBC) (deposition date: 2012-12-28, release date: 2013-02-20, Last modification date: 2023-09-20)

Primary citation

Pryor, E.E.,Horanyi, P.S.,Clark, K.M.,Fedoriw, N.,Connelly, S.M.,Koszelak-Rosenblum, M.,Zhu, G.,Malkowski, M.G.,Wiener, M.C.,Dumont, M.E.
Structure of the integral membrane protein CAAX protease Ste24p.
Science, 339:1600-1604, 2013

PubMed 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.

PubMed: 23539602
DOI: 10.1126/science.1232048

Experimental method

X-RAY DIFFRACTION (3.102 Å)