4IL3

Crystal Structure of S. mikatae Ste24p

4IL3 の概要

• エントリーDOI: 10.2210/pdb4il3/pdb
• 分子名称: Ste24p, ZINC ION (2 entities in total)
• 機能のキーワード: membrane protein, alpha helical, caax protease, a-factor, structural genomics, mpsbc, psi-biology, membrane protein structural biology consortium, hydrolase
• 由来する生物種: Saccharomyces mikatae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 106810.79

構造登録者

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) (登録日: 2012-12-28, 公開日: 2013-02-20, 最終更新日: 2023-09-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.102 Å)