4CMN
Crystal structure of OCRL in complex with a phosphate ion
Summary for 4CMN
| Entry DOI | 10.2210/pdb4cmn/pdb |
| Related | 4CML |
| Descriptor | INOSITOL POLYPHOSPHATE 5-PHOSPHATASE OCRL-1, PHOSPHATE ION, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | hydrolase, inositol signalling, sgc stockholm, structural genomics consortium, lowe syndrome, dent disease |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Cytoplasmic vesicle, phagosome membrane (By similarity): Q01968 |
| Total number of polymer chains | 1 |
| Total formula weight | 41845.08 |
| Authors | 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. (deposition date: 2014-01-16, release date: 2014-04-16, Last modification date: 2023-12-20) |
| Primary citation | 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 Cited by 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: 24704254DOI: 10.1016/J.STR.2014.01.013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.13 Å) |
Structure validation
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