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PDBsum entry 3of1

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protein ligands links
Transferase PDB id
3of1

 

 

 

 

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Contents
Protein chain
246 a.a. *
Ligands
CMP ×2
Waters ×93
* Residue conservation analysis
PDB id:
3of1
Name: Transferase
Title: Crystal structure of bcy1, the yeast regulatory subunit of pka
Structure: Camp-dependent protein kinase regulatory subunit. Chain: a. Fragment: camp 1 and camp 2 nucleotide binding regions. Synonym: pka regulatory subunit. Engineered: yes
Source: Saccharomyces cerevisiae. Yeast. Organism_taxid: 4932. Gene: bcy1, reg1, sra1, yil033c. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.21Å     R-factor:   0.200     R-free:   0.263
Authors: J.Rinaldi,J.Wu,J.Yang,C.Y.Ralston,B.Sankaran,S.Moreno,S.S.Taylor
Key ref: J.Rinaldi et al. (2010). Structure of yeast regulatory subunit: a glimpse into the evolution of PKA signaling. Structure, 18, 1471-1482. PubMed id: 21070946
Date:
13-Aug-10     Release date:   01-Dec-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P07278  (KAPR_YEAST) -  cAMP-dependent protein kinase regulatory subunit from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
416 a.a.
246 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Structure 18:1471-1482 (2010)
PubMed id: 21070946  
 
 
Structure of yeast regulatory subunit: a glimpse into the evolution of PKA signaling.
J.Rinaldi, J.Wu, J.Yang, C.Y.Ralston, B.Sankaran, S.Moreno, S.S.Taylor.
 
  ABSTRACT  
 
The major cAMP receptors in eukaryotes are the regulatory (R) subunits of PKA, an allosteric enzyme conserved in fungi through mammals. While mammals have four R-subunit genes, Saccharomyces cerevisiae has only one, Bcy1. To achieve a molecular understanding of PKA activation in yeast and to explore the evolution of cyclic-nucleotide binding (CNB) domains, we solved the structure of cAMP-bound Bcy1(168-416). Surprisingly, the relative orientation of the two CNB domains in Bcy1 is very different from mammalian R-subunits. This quaternary structure is defined primarily by a fungi-specific sequence in the hinge between the αB/αC helices of the CNB-A domain. The unique interface between the two CNB domains in Bcy1 defines the allosteric mechanism for cooperative activation of PKA by cAMP. Some interface motifs are isoform-specific while others, although conserved, play surprisingly different roles in each R-subunit. Phylogenetic analysis shows that structural differences in Bcy1 are shared by fungi of the subphylum Saccharomycotina.
 

 

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