PDBsum entry 3pfq

Transferase

PDB id: 3pfq

Contents

Protein chain

523 a.a. *

Ligands

ANP

Metals

_CA ×3

_ZN ×2

* Residue conservation analysis

PDB id:

3pfq

Name:

Transferase

Title:

Crystal structure and allosteric activation of protein kinasE C beta ii

Structure:

Protein kinasE C beta type. Chain: a. Fragment: pkc beta ii. Synonym: pkc-beta. Engineered: yes. Mutation: yes

Source:

Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: prkcb, pkcb, prkcb1. Expressed in: trichoplusia ni. Expression_system_taxid: 7111

Resolution:

4.00Å R-factor: 0.193 R-free: 0.245

Authors:

T.A.Leonard,B.Rozycki,L.F.Saidi,G.Hummer,J.H.Hurley

Key ref:

T.A.Leonard et al. (2011). Crystal structure and allosteric activation of protein kinase C βII. Cell, 144, 55-66. PubMed id: 21215369

Date:

28-Oct-10 Release date: 02-Feb-11

Protein chain

P68403  (KPCB_RAT) -  Protein kinase C beta type from Rattus norvegicus

Seq: 671 a.a.

Struc: 523 a.a.*

* PDB and UniProt seqs differ at 27 residue positions (black crosses)

Enzyme reactions

• Enzyme class: 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⁺

L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] (Bound ligand (Het Group name = ANP) matches with 81.25% similarity) + ADP + H(+)

L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] (Bound ligand (Het Group name = ANP) matches with 81.25% similarity) + ADP + H(+)

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

reference

Cell 144:55-66 (2011)

PubMed id: 21215369

Crystal structure and allosteric activation of protein kinase C βII.

T.A.Leonard, B.Różycki, L.F.Saidi, G.Hummer, J.H.Hurley.

ABSTRACT

Protein kinase C (PKC) isozymes are the paradigmatic effectors of lipid signaling. PKCs translocate to cell membranes and are allosterically activated upon binding of the lipid diacylglycerol to their C1A and C1B domains. The crystal structure of full-length protein kinase C βII was determined at 4.0 Å, revealing the conformation of an unexpected intermediate in the activation pathway. Here, the kinase active site is accessible to substrate, yet the conformation of the active site corresponds to a low-activity state because the ATP-binding side chain of Phe629 of the conserved NFD motif is displaced. The C1B domain clamps the NFD helix in a low-activity conformation, which is reversed upon membrane binding. A low-resolution solution structure of the closed conformation of PKCβII was derived from small-angle X-ray scattering. Together, these results show how PKCβII is allosterically regulated in two steps, with the second step defining a novel protein kinase regulatory mechanism.