PDBsum entry 1i09

Transferase

PDB id: 1i09

Contents

Protein chain

338 a.a. *

Ligands

PO4 ×4

Waters ×46

* Residue conservation analysis

PDB id:

1i09

Name:

Transferase

Title:

Structure of glycogen synthase kinase-3 (gsk3b)

Structure:

Glycogen synthase kinase-3 beta. Chain: a, b. Synonym: gsk-3 beta, gsk3b. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: unidentified baculovirus. Expression_system_taxid: 10469

Biol. unit:

Dimer (from PQS)

Resolution:

2.70Å R-factor: 0.242 R-free: 0.274

Authors:

E.Ter Haar,J.T.Coll,J.Jain

Key ref:

E.ter Haar et al. (2001). Structure of GSK3beta reveals a primed phosphorylation mechanism. Nat Struct Biol, 8, 593-596. PubMed id: 11427888 DOI: 10.1038/89624

Date:

29-Jan-01 Release date: 01-Jan-02

Protein chains

P49841  (GSK3B_HUMAN) -  Glycogen synthase kinase-3 beta from Homo sapiens

Seq: 420 a.a.

Struc: 338 a.a.

Enzyme reactions

• Enzyme class 1: 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⁺
• Enzyme class 2: E.C.2.7.11.26 - [tau protein] kinase.
• Reaction:
  1. L-seryl-[tau protein] + ATP = O-phospho-L-seryl-[tau protein] + ADP + H⁺
  2. L-threonyl-[tau protein] + ATP = O-phospho-L-threonyl-[tau 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: 10.1038/89624

Nat Struct Biol 8:593-596 (2001)

PubMed id: 11427888

Structure of GSK3beta reveals a primed phosphorylation mechanism.

E.ter Haar, J.T.Coll, D.A.Austen, H.M.Hsiao, L.Swenson, J.Jain.

ABSTRACT

GSK3beta was identified as the kinase that phosphorylates glycogen synthase but is now known to be involved in multiple signaling pathways. GSK3beta prefers prior phosphorylation of its substrates. We present the structure of unphosphorylated GSK3beta at 2.7 A. The orientation of the two domains and positioning of the activation loop of GSK3beta are similar to those observed in activated kinases. A phosphate ion held by Arg 96, Arg 180 and Lys 205 occupies the same position as the phosphate group of the phosphothreonine in activated p38gamma, CDK2 or ERK2. A loop from a neighboring molecule in the crystal occupies a portion of the substrate binding groove. The structure explains the unique primed phosphorylation mechanism of GSK3beta and how GSK3beta relies on a phosphoserine in the substrate for the alignment of the beta- and alpha-helical domains.

Selected figure(s)

Figure 1.
Figure 1. Representative portion of a 2F[o] - F[c] electron density map contoured at 1.5 .

Figure 4.
Figure 4. The GSK3 substrate binding groove.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2001, 8, 593-596) copyright 2001.

Figures were selected by an automated process.