PDBsum entry: 1bo1

Transferase

PDB id: 1bo1

Contents

Protein chains

326 a.a. *

Waters ×19

* Residue conservation analysis

PDB id:

1bo1

Name:

Transferase

Title:

Phosphatidylinositol phosphate kinase type ii beta

Structure:

Protein (phosphatidylinositol phosphate kinase iibeta). Chain: a, b. Synonym: pipk. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_cell_line: bl21(de3). Other_details: human enzyme cloned into e.Coli.

Biol. unit:

Dimer (from PQS)

Resolution:

3.00Å R-factor: 0.229 R-free: 0.299

Authors:

V.D.Rao,S.Misra,I.V.Boronenkov,R.A.Anderson,J.H.Hurley

Key ref:

V.D.Rao et al. (1998). Structure of type IIbeta phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation. Cell, 94, 829-839. PubMed id: 9753329 DOI: 10.1016/S0092-8674(00)81741-9

Date:

02-Aug-98 Release date: 07-Oct-98

Protein chains

P78356  (PI42B_HUMAN) -  Phosphatidylinositol-5-phosphate 4-kinase type-2 beta

Seq: 416 a.a.

Struc: 326 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.1.149 - 1-phosphatidylinositol-5-phosphate 4-kinase.
• Pathway: 1-Phosphatidyl-myo-inositol Metabolism
• Reaction: ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate = ADP + 1-phosphatidyl- 1D-myo-inositol 4,5-bisphosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Cellular component: membrane (6 terms)
• Biological process: cell surface receptor linked signaling pathway (4 terms)
• Biochemical function: nucleotide binding (8 terms)

reference

DOI no: 10.1016/S0092-8674(00)81741-9

Cell 94:829-839 (1998)

PubMed id: 9753329

Structure of type IIbeta phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation.

V.D.Rao, S.Misra, I.V.Boronenkov, R.A.Anderson, J.H.Hurley.

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.

Selected figure(s)

Figure 1.
Figure 1. Tertiary and Quaternary Structure of PIPKIIβ(A) Ribbon drawing of PIPKIIβ monomer prepared with MOLSCRIPT ([34]) and Raster3D ( [40]).(B) Schematic of the PIPKIIβ fold. The conserved ATP-binding core elements are colored green.(C) Ribbon representation of the PIPKIIβ dimer. The subunits are colored yellow (molecule A) and red (molecule B).

Figure 3.
Figure 3. Molecular Surface of the PIPKIIβ DimerThe surface is colored according to electrostatic potential using GRASP ([42]) in (A) sagittal and (B) normal projections relative to the presumed plane of the membrane. Saturating red indicated φ < −10 kT/e, and saturating blue indicates φ > 10 kT/e, where T = 293°K. ATP and the inositol (1,5) bisphosphate moiety of the PI5P headgroup are shown in yellow bonds docked into one of the two active sites. (C) Docking of PIPKIIβ dimer onto a membrane surface, using the DMPC crystal structure as a model. The asterisk and arrow indicate the putative TNF receptor–binding site.

The above figures are reprinted by permission from Cell Press: Cell (1998, 94, 829-839) copyright 1998.

Figures were selected by an automated process.