PDBsum entry 4mjs

Transferase/protein binding

PDB id: 4mjs

Contents

Protein chains

(+ 6 more) 88 a.a.

82 a.a.

84 a.a.

87 a.a.

Ligands

EDO ×4

Waters ×397

PDB id:

4mjs

Name:

Transferase/protein binding

Title:

Crystal structure of a pb1 complex

Structure:

Protein kinasE C zeta type. Chain: a, c, e, g, i, k, m, o, q, s, u, w. Fragment: pb1 domain, unp residues 15-101. Synonym: npkc-zeta. Engineered: yes. Sequestosome-1. Chain: b, d, f, h, j, l, n, p, r, t, v, x. Fragment: pb1 domain, unp residues 3-102. Synonym: ebi3-associated protein of 60 kda, ebiap, p60,

Source:

Rattus norvegicus. Brown rat,rat,rats. Organism_taxid: 10116. Gene: pkcz, prkcz. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens. Human. Organism_taxid: 9606.

Resolution:

2.50Å R-factor: 0.240 R-free: 0.287

Authors:

J.Ren,Z.X.Wang,J.W.Wu

Key ref:

J.Ren et al. (2014). Structural and biochemical insights into the homotypic PB1-PB1 complex between PKCζ and p62. Sci China Life Sci, 57, 69-80. PubMed id: 24369353 DOI: 10.1007/s11427-013-4592-z

Date:

04-Sep-13 Release date: 27-Aug-14

Protein chains

P09217  (KPCZ_RAT) -  Protein kinase C zeta type from Rattus norvegicus

Seq: 592 a.a.

Struc: 88 a.a.*

Protein chains

Q13501  (SQSTM_HUMAN) -  Sequestosome-1 from Homo sapiens

Seq: 440 a.a.

Struc: 82 a.a.*

Protein chains

Q13501  (SQSTM_HUMAN) -  Sequestosome-1 from Homo sapiens

Seq: 440 a.a.

Struc: 84 a.a.*

Protein chains

Q13501  (SQSTM_HUMAN) -  Sequestosome-1 from Homo sapiens

Seq: 440 a.a.

Struc: 87 a.a.*

* PDB and UniProt seqs differ at 9 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, C, E, G, I, K, M, O, Q, S, U, W: 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: 10.1007/s11427-013-4592-z

Sci China Life Sci 57:69-80 (2014)

PubMed id: 24369353

Structural and biochemical insights into the homotypic PB1-PB1 complex between PKCζ and p62.

J.Ren, J.Wang, Z.Wang, J.Wu.

ABSTRACT

The atypical PKC isoforms (ζ and ı) play essential roles in regulating various cellular processes. Both the hetero-interaction between PKCζ and p62 through their N-terminal PB1 domains and the homo-oligomerization of p62 via its PB1 domain are critical for the activation of NF-κB signaling; however, the molecular mechanisms concerning the formation and regulation of these homotypic complexes remain unclear. Here we determined the crystal structure of PKCζ-PB1 in complex with a monomeric p62-PB1 mutant, where the massive electrostatic interactions between the acidic OPCA motif of PKCζ-PB1 and the basic surface of p62-PB1, as well as additional hydrogen bonds, ensure the formation of a stable and specific complex. The PKCζ-p62 interaction is interfered with the modification of a specific Cys of PKCζ by the antiarthritis drug aurothiomalate, though all four cysteine residues in the PKCζ-PB1 domain can be modified in in vitro assay. In addition, detailed structural and biochemical analyses demonstrate that the PB1 domains of aPKCs belong to the type I group, which can depolymerize the high-molecular-weight p62 aggregates into homo-oligomers of lower order. These data together unravel the molecular mechanisms of the homo-or hetero-interactions between p62 and PKCζ and provide the basis for designing inhibitors of NF-κB signaling.