PDBsum entry 1j1c

Transferase

PDB id: 1j1c

Contents

Protein chain

354 a.a. *

Ligands

ADP ×2

Metals

_MG ×2

Waters ×267

* Residue conservation analysis

PDB id:

1j1c

Name:

Transferase

Title:

Binary complex structure of human tau protein kinase i with adp

Structure:

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

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Dimer (from PQS)

Resolution:

2.10Å R-factor: 0.218 R-free: 0.242

Authors:

M.Aoki,T.Yokota,I.Sugiura,C.Sasaki,T.Hasegawa,C.Okumura,T.Kohno, S.Sugio,T.Matsuzaki

Key ref:

M.Aoki et al. (2004). Structural insight into nucleotide recognition in tau-protein kinase I/glycogen synthase kinase 3 beta. Acta Crystallogr D Biol Crystallogr, 60, 439-446. PubMed id: 14993667 DOI: 10.1107/S090744490302938X

Date:

03-Dec-02 Release date: 03-Dec-03

Protein chains

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

Seq: 420 a.a.

Struc: 354 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⁺

L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] (Bound ligand (Het Group name = ADP) corresponds exactly) + ADP + H(+)

L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] (Bound ligand (Het Group name = ADP) corresponds exactly) + 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⁺

L-seryl-[tau protein] + ATP = O-phospho-L-seryl-[tau protein] (Bound ligand (Het Group name = ADP) corresponds exactly) + ADP + H(+)

L-threonyl-[tau protein] + ATP = O-phospho-L-threonyl-[tau protein] (Bound ligand (Het Group name = ADP) corresponds exactly) + 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/S090744490302938X

Acta Crystallogr D Biol Crystallogr 60:439-446 (2004)

PubMed id: 14993667

Structural insight into nucleotide recognition in tau-protein kinase I/glycogen synthase kinase 3 beta.

M.Aoki, T.Yokota, I.Sugiura, C.Sasaki, T.Hasegawa, C.Okumura, K.Ishiguro, T.Kohno, S.Sugio, T.Matsuzaki.

ABSTRACT

Human tau-protein kinase I (TPK I; also known as glycogen synthase kinase 3 beta; GSK3 beta) is a serine/threonine protein kinase that participates in Alzheimer's disease. Here, binary complex structures of full-length TPK I/GSK3 beta with the ATP analogues ADP and AMPPNP solved by the X-ray diffraction method at 2.1 and 1.8 A resolution, respectively, are reported. TPK I/GSK3 beta is composed of three domains: an N-terminal domain consisting of a closed beta-barrel structure, a C-terminal domain containing a 'kinase fold' structure and a small extra-domain subsequent to the C-terminal domain. The catalytic site is between the two major domains and has an ATP-analogue molecule in its ATP-binding site. The adenine ring is buried in the hydrophobic pocket and interacts specifically with the main-chain atoms of the hinge loop. The overall structure and substrate-binding residues are similar to those observed in other Ser/Thr protein kinases, while Arg141 (which is not conserved among other Ser/Thr protein kinases) is one of the key residues for specific ATP/ADP recognition by TPK I/GSK3 beta. No residues are phosphorylated, while the orientation of the activation loop in TPK I/GSK3 beta is similar to that in phosphorylated CDK2 and ERK2, suggesting that TPK I/GSK3 beta falls into a conformation that enables it to be constitutively active.

Selected figure(s)

Figure 3.
Figure 3 Residues participating in binding of (a) ADP and (b) AMPPNP in the ATP-binding site of GSK3 . GSK3 is drawn as a white ribbon; amino-acid residues, ATP analogues, magnesium ion and water molecules are shown as black sticks, grey sticks, a black sphere and light grey spheres, respectively. Hydrogen bonds are shown as dotted lines. These figures were produced using the program MOLSCRIPT.

Figure 4.
Figure 4 Magnesium-binding site in (a) the GSK3 -ADP complex and (b) the GSK3 -AMPPNP complex. GSK3 is drawn as a white ribbon; amino-acid residues, ATP analogues, magnesium ion and water molecules are shown as black sticks, grey sticks, a black sphere and light grey spheres, respectively. Hydrogen bonds are shown as dotted lines. These figures were produced using the program MOLSCRIPT.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2004, 60, 439-446) copyright 2004.

Figures were selected by an automated process.