4CMN

Crystal structure of OCRL in complex with a phosphate ion

4CMN の概要

• エントリーDOI: 10.2210/pdb4cmn/pdb
• 関連するPDBエントリー: 4CML
• 分子名称: INOSITOL POLYPHOSPHATE 5-PHOSPHATASE OCRL-1, PHOSPHATE ION, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, inositol signalling, sgc stockholm, structural genomics consortium, lowe syndrome, dent disease
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasmic vesicle, phagosome membrane (By similarity): Q01968
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41845.08

構造登録者

Tresaugues, L.,Moche, M.,Arrowsmith, C.H.,Berglund, H.,Bountra, C.,Edwards, A.M.,Ekblad, T.,Flodin, S.,Graslund, S.,Karlberg, T.,Nyman, T.,Schuler, H.,Silvander, C.,Thorsell, A.G.,Weigelt, J.,Welin, M.,Nordlund, P. (登録日: 2014-01-16, 公開日: 2014-04-16, 最終更新日: 2023-12-20)

主引用文献

Tresaugues, L.,Silvander, C.,Flodin, S.,Welin, M.,Nyman, T.,Graslund, S.,Hammarstrom, M.,Berglund, H.,Nordlund, P.
Structural Basis for Phosphoinositide Substrate Recognition, Catalysis, and Membrane Interactions in Human Inositol Polyphosphate 5-Phosphatases.
Structure, 22:744-, 2014

PubMed Abstract: SHIP2, OCRL, and INPP5B belong to inositol polyphosphate 5-phophatase subfamilies involved in insulin regulation and Lowes syndrome. The structural basis for membrane recognition, substrate specificity, and regulation of inositol polyphosphate 5-phophatases is still poorly understood. We determined the crystal structures of human SHIP2, OCRL, and INPP5B, the latter in complex with phosphoinositide substrate analogs, which revealed a membrane interaction patch likely to assist in sequestering substrates from the lipid bilayer. Residues recognizing the 1-phosphate of the substrates are highly conserved among human family members, suggesting similar substrate binding modes. However, 3- and 4-phosphate recognition varies and determines individual substrate specificity profiles. The high conservation of the environment of the scissile 5-phosphate suggests a common reaction geometry for all members of the human 5-phosphatase family.

PubMed: 24704254
DOI: 10.1016/J.STR.2014.01.013

実験手法

X-RAY DIFFRACTION (3.13 Å)