1BO1

PHOSPHATIDYLINOSITOL PHOSPHATE KINASE TYPE II BETA

Summary for 1BO1

• Entry DOI: 10.2210/pdb1bo1/pdb
• Descriptor: PROTEIN (PHOSPHATIDYLINOSITOL PHOSPHATE KINASE IIBETA) (2 entities in total)
• Functional Keywords: lipid signaling, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 94895.85

Authors

Rao, V.D.,Misra, S.,Boronenkov, I.V.,Anderson, R.A.,Hurley, J.H. (deposition date: 1998-08-02, release date: 1998-10-07, Last modification date: 2024-02-07)

Primary citation

Rao, V.D.,Misra, S.,Boronenkov, I.V.,Anderson, R.A.,Hurley, J.H.
Structure of type IIbeta phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation.
Cell(Cambridge,Mass.), 94:829-839, 1998

PubMed Abstract: Phosphoinositide kinases play central roles in signal transduction by phosphorylating the inositol ring at specific positions. The structure of one such enzyme, type IIbeta phosphatidylinositol phosphate kinase, reveals a protein kinase ATP-binding core and demonstrates that all phosphoinositide kinases belong to one superfamily. The enzyme is a disc-shaped homodimer with a 33 x 48 A basic flat face that suggests an electrostatic mechanism for plasma membrane targeting. Conserved basic residues form a putative phosphatidylinositol phosphate specificity site. The substrate-binding site is open on one side, consistent with dual specificity for phosphatidylinositol 3- and 5-phosphates. A modeled complex with membrane-bound substrate and ATP shows how a phosphoinositide kinase can phosphorylate its substrate in situ at the membrane interface.

PubMed: 9753329
DOI: 10.1016/S0092-8674(00)81741-9

Experimental method

X-RAY DIFFRACTION (3 Å)