PDBsum entry 4zdr

Protein binding

PDB id: 4zdr

Contents

Protein chains

243 a.a.

Ligands

GOL ×3

SO4 ×2

TME ×6

Waters ×8

PDB id:

4zdr

Name:

Protein binding

Title:

Crystal structure of 14-3-3[zeta]-lkb1 fusion protein

Structure:

14-3-3 protein zeta/delta,ggsggs linker,serine/threonine- protein kinase stk11. Chain: a, b. Fragment: unp residues 1-230,unp residues 333-340. Synonym: protein kinasE C inhibitor protein 1,kcip-1,liver kinase b1, hlkb1,renal carcinoma antigen ny-ren-19. Engineered: yes. Mutation: yes

Source:

Homo sapiens, synthetic construct. Human. Organism_taxid: 9606, 32630. Gene: ywhaz, stk11, lkb1, pjs. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: codonplus

Resolution:

2.90Å R-factor: 0.196 R-free: 0.245

Authors:

S.Ding,Z.B.Shi

Key ref:

S.Ding et al. (2015). Structure of the 14-3-3ζ-LKB1 fusion protein provides insight into a novel ligand-binding mode of 14-3-3. Acta Crystallogr F Struct Biol Commun, 71, 1114-1119. PubMed id: 26323294 DOI: 10.1107/S2053230X15012595

Date:

18-Apr-15 Release date: 09-Sep-15

Protein chains

P63104  (1433Z_HUMAN) -  14-3-3 protein zeta/delta from Homo sapiens

Seq: 245 a.a.

Struc: 243 a.a.*

Protein chains

Q15831  (STK11_HUMAN) -  Serine/threonine-protein kinase STK11 from Homo sapiens

Seq: 433 a.a.

Struc: 243 a.a.*

* PDB and UniProt seqs differ at 231 residue positions (black crosses)

Enzyme reactions

• Enzyme class 1: E.C.?
• Enzyme class 2: E.C.2.7.11.1 - non-specific serine/threonine protein kinase.
• 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⁺

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

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

reference

DOI no: 10.1107/S2053230X15012595

Acta Crystallogr F Struct Biol Commun 71:1114-1119 (2015)

PubMed id: 26323294

Structure of the 14-3-3ζ-LKB1 fusion protein provides insight into a novel ligand-binding mode of 14-3-3.

S.Ding, R.Zhou, Y.Zhu.

ABSTRACT

The 14-3-3 proteins are a family of highly conserved proteins that play key roles in many cellular processes. The tumour suppressor LKB1 regulates cell polarity, cell growth and energy metabolism. 14-3-3 proteins bind to LKB1 and suppress its functions. Previously, preliminary crystallographic data for the 14-3-3ζ-LKB1 fusion protein have been reported. Here, the crystal structure of this fusion protein was solved and a novel potential binding mode of 14-3-3 to its ligands was found.