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PDBsum entry 3of1
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* Residue conservation analysis
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PDB id:
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Transferase
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Title:
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Crystal structure of bcy1, the yeast regulatory subunit of pka
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Structure:
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Camp-dependent protein kinase regulatory subunit. Chain: a. Fragment: camp 1 and camp 2 nucleotide binding regions. Synonym: pka regulatory subunit. Engineered: yes
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Source:
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Saccharomyces cerevisiae. Yeast. Organism_taxid: 4932. Gene: bcy1, reg1, sra1, yil033c. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.21Å
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R-factor:
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0.200
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R-free:
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0.263
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Authors:
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J.Rinaldi,J.Wu,J.Yang,C.Y.Ralston,B.Sankaran,S.Moreno,S.S.Taylor
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Key ref:
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J.Rinaldi
et al.
(2010).
Structure of yeast regulatory subunit: a glimpse into the evolution of PKA signaling.
Structure,
18,
1471-1482.
PubMed id:
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Date:
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13-Aug-10
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Release date:
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01-Dec-10
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PROCHECK
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Headers
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References
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P07278
(KAPR_YEAST) -
cAMP-dependent protein kinase regulatory subunit from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq: Struc:
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416 a.a.
246 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Structure
18:1471-1482
(2010)
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PubMed id:
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Structure of yeast regulatory subunit: a glimpse into the evolution of PKA signaling.
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J.Rinaldi,
J.Wu,
J.Yang,
C.Y.Ralston,
B.Sankaran,
S.Moreno,
S.S.Taylor.
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ABSTRACT
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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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}
}
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