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1bkx

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[[Image:1bkx.gif|left|200px]]
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{{STRUCTURE_1bkx| PDB=1bkx | SCENE= }}
{{STRUCTURE_1bkx| PDB=1bkx | SCENE= }}
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'''A BINARY COMPLEX OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE AND ADENOSINE FURTHER DEFINES CONFORMATIONAL FLEXIBILITY'''
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===A BINARY COMPLEX OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE AND ADENOSINE FURTHER DEFINES CONFORMATIONAL FLEXIBILITY===
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==Overview==
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BACKGROUND: cAMP-dependent protein kinase (cAPK), a ubiquitous protein in eukaryotic cells, is one of the simplest members of the protein kinase family. It was the first protein kinase to be crystallized and continues to serve as a biochemical and structural prototype for this family of enzymes. To further understand the conformational changes that occur in different liganded and unliganded states of cAPK, the catalytic subunit of cAPK was crystallized in the absence of peptide inhibitor. RESULTS: The crystal structure of the catalytic subunit of mouse recombinant cAPK (rC) complexed with adenosine was solved at 2.6 A resolution and refined to a crystallographic R factor of 21.9% with good stereochemical parameters. This is the first structure of the rC subunit that lacks a bound inhibitor or substrate peptide. The structure was solved by molecular replacement and comprises two lobes (large and small) which contain a number of conserved loops. CONCLUSIONS: The binary complex of rC and adenosine adopts an 'intermediate' conformation relative to the previously described 'closed' and 'open' conformations of other rC complexes. Based on a comparison of these structures, the induced fit that is necessary for catalysis and closing of the active-site cleft appears to be confined to the small lobe, as in the absence of the peptide the conformation of the large lobe, including the peptide-docking surface, does not change. Three specific components contribute to the closing of the cleft: rotation of the small lobe; movement of the C-terminal tail; and closing of the so-called glycine-rich loop. There is no induced fit in the large lobe to accommodate the peptide and the closing of the cleft. A portion of the C-terminal tail, residues 315-334, serves as a gate for the entry or exit of the nucleotide into the hydrophobic active-site cleft.
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(as it appears on PubMed at http://www.pubmed.gov), where 9261084 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9261084}}
==About this Structure==
==About this Structure==
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[[Category: Protein kinase]]
[[Category: Protein kinase]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:38:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:19:24 2008''

Revision as of 16:19, 30 June 2008

Image:1bkx.png

Template:STRUCTURE 1bkx

A BINARY COMPLEX OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE AND ADENOSINE FURTHER DEFINES CONFORMATIONAL FLEXIBILITY

Template:ABSTRACT PUBMED 9261084

About this Structure

1BKX is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

A binary complex of the catalytic subunit of cAMP-dependent protein kinase and adenosine further defines conformational flexibility., Narayana N, Cox S, Nguyen-huu X, Ten Eyck LF, Taylor SS, Structure. 1997 Jul 15;5(7):921-35. PMID:9261084

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