PDBsum entry 1wmh

Transferase/cell cycle

PDB id: 1wmh

Contents

Protein chains

83 a.a. *

82 a.a. *

Waters ×188

* Residue conservation analysis

PDB id:

1wmh

Name:

Transferase/cell cycle

Title:

Crystal structure of a pb1 domain complex of protein kinasE C iota and par6 alpha

Structure:

Protein kinasE C, iota type. Chain: a. Fragment: pb1 domain. Synonym: npkc-iota, atypical protein kinasE C-lambda/iota, apkc- lambda/iota. Engineered: yes. Partitioning defective-6 homolog alpha. Chain: b. Fragment: pb1 domain.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: pkciota. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Gene: par6alpha.

Biol. unit:

Tetramer (from PQS)

Resolution:

1.50Å R-factor: 0.216 R-free: 0.224

Authors:

Y.Hirano,S.Yoshinaga,N.N.Suzuki,M.Horiuchi,M.Kohjima,R.Takeya, H.Sumimoto,F.Inagaki

Key ref:

Y.Hirano et al. (2005). Structure of a cell polarity regulator, a complex between atypical PKC and Par6 PB1 domains. J Biol Chem, 280, 9653-9661. PubMed id: 15590654 DOI: 10.1074/jbc.M409823200

Date:

09-Jul-04 Release date: 07-Dec-04

Protein chain

P41743  (KPCI_HUMAN) -  Protein kinase C iota type from Homo sapiens

Seq: 596 a.a.

Struc: 83 a.a.

Protein chain

Q9NPB6  (PAR6A_HUMAN) -  Partitioning defective 6 homolog alpha from Homo sapiens

Seq: 346 a.a.

Struc: 82 a.a.

Enzyme reactions

• Enzyme class: Chain A: E.C.2.7.11.13 - protein kinase C.
• Reaction:
  1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
  2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺

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

reference

DOI no: 10.1074/jbc.M409823200

J Biol Chem 280:9653-9661 (2005)

PubMed id: 15590654

Structure of a cell polarity regulator, a complex between atypical PKC and Par6 PB1 domains.

Y.Hirano, S.Yoshinaga, R.Takeya, N.N.Suzuki, M.Horiuchi, M.Kohjima, H.Sumimoto, F.Inagaki.

ABSTRACT

A complex of atypical PKC and Par6 is a common regulator for cell polarity-related processes, which is an essential clue to evolutionary conserved cell polarity regulation. Here, we determined the crystal structure of the complex of PKCiota and Par6alpha PB1 domains to a resolution of 1.5 A. Both PB1 domains adopt a ubiquitin fold. PKCiota PB1 presents an OPR, PC, and AID (OPCA) motif, 28 amino acid residues with acidic and hydrophobic residues, which interacts with the conserved lysine residue of Par6alpha PB1 in a front and back manner. On the interface, several salt bridges are formed including the conserved acidic residues on the OPCA motif of PKCiota PB1 and the conserved lysine residue on the Par6alpha PB1. Structural comparison of the PKCiota and Par6alpha PB1 complex with the p40phox and p67phox PB1 domain complex, subunits of neutrophil NADPH oxidase, reveals that the specific interaction is achieved by tilting the interface so that the insertion or extension in the sequence is engaged in the specificity determinant. The PB1 domain develops the interaction surface on the ubiquitin fold to increase the versatility of molecular interaction.

Selected figure(s)

Figure 3.
FIG. 3. Detailed molecular interaction between PKC[ ]PB1 and Par6 PB1. A, ribbon and stick diagrams of a PB1 complex of PKC[ ]-Par6 represented in an open book style. The two acidic regions of PKC[ ]PB1 and the two basic regions of Par6 PB1 in the interaction surface are encircled in red and blue, respectively. B, PKC[ ]-Par6 interface with the corresponding final 2|F[o]| - |F[c]| electron density at 2.0 is shown. A1, A2, B1, and B2' indicate the same as in A. Orange dotted lines indicate intermolecular hydrogen bonds, and blue dotted lines indicate intramolecular hydrogen bonds. C, a stick model of manifold salt bridge network in the interaction surface. Blue spheres represent water molecules. Orange dotted lines indicate intermolecular hydrogen bonds, and blue dotted lines indicate intramolecular hydrogen bonds or water molecule-mediated hydrogen bonds.

Figure 5.
FIG. 5. General interaction surface of the PB1 domain. Electrostatic surface potentials of the interaction surfaces of type I and type II PB1 domains are presented. The conserved acidic regions of the type I PB1 domain, A1 and A2, are encircled in orange, and the conserved basic regions of the type II PB1 domain, B1and B2/B2', are encircled in blue.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2005, 280, 9653-9661) copyright 2005.

Figures were selected by an automated process.