PDBsum entry 1fot

Transferase

PDB id: 1fot

Contents

Protein chain

300 a.a. *

Waters ×2

* Residue conservation analysis

PDB id:

1fot

Name:

Transferase

Title:

Structure of the unliganded camp-dependent protein kinase catalytic subunit from saccharomyces cerevisiae

Structure:

Camp-dependent protein kinase type 1. Chain: a. Fragment: n-terminus truncated tpk1. Synonym: tpk1 delta. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932. Other_details: saccharomyces cerevisiae

Resolution:

2.80Å R-factor: 0.194 R-free: 0.243

Authors:

N.Mashhoon,G.Carmel,J.W.Pflugrath,J.Kuret

Key ref:

N.Mashhoon et al. (2001). Structure of the unliganded cAMP-dependent protein kinase catalytic subunit from Saccharomyces cerevisiae. Arch Biochem Biophys, 387, 11-19. PubMed id: 11368172 DOI: 10.1006/abbi.2000.2241

Date:

28-Aug-00 Release date: 13-Jun-01

Protein chain

P06244  (KAPA_YEAST) -  cAMP-dependent protein kinase type 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 397 a.a.

Struc: 300 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.2.7.11.11 - cAMP-dependent 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⁺

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

reference

DOI no: 10.1006/abbi.2000.2241

Arch Biochem Biophys 387:11-19 (2001)

PubMed id: 11368172

Structure of the unliganded cAMP-dependent protein kinase catalytic subunit from Saccharomyces cerevisiae.

N.Mashhoon, G.Carmel, J.W.Pflugrath, J.Kuret.

ABSTRACT

The structure of TPK1delta, a truncated variant of the cAMP-dependent protein kinase catalytic subunit from Saccharomyces cerevisiae, was determined in an unliganded state at 2.8 A resolution and refined to a crystallographic R-factor of 19.4%. Comparison of this structure to that of its fully liganded mammalian homolog revealed a highly conserved protein fold comprised of two globular lobes. Within each lobe, root mean square deviations in Calpha positions averaged approximately equals 0.9 A. In addition, a phosphothreonine residue was found in the C-terminal domain of each enzyme. Further comparison of the two structures suggests that a trio of conformational changes accompanies ligand-binding. The first consists of a 14.7 degrees rigid-body rotation of one lobe relative to the other and results in closure of the active site cleft. The second affects only the glycine-rich nucleotide binding loop, which moves approximately equals 3 A to further close the active site and traps the nucleotide substrate. The third is localized to a C-terminal segment that makes direct contact with ligands and the ligand-binding cleft. In addition to resolving the conformation of unliganded enzyme, the model shows that the salient features of the cAMP-dependent protein kinase are conserved over long evolutionary distances.