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1fot
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(New page: 200px<br /><applet load="1fot" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fot, resolution 2.80Å" /> '''STRUCTURE OF THE UNL...)
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Revision as of 12:58, 20 November 2007
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STRUCTURE OF THE UNLIGANDED CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT FROM SACCHAROMYCES CEREVISIAE
Overview
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.
About this Structure
1FOT is a Single protein structure of sequence from Saccharomyces cerevisiae. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
Structure of the unliganded cAMP-dependent protein kinase catalytic subunit from Saccharomyces cerevisiae., Mashhoon N, Carmel G, Pflugrath JW, Kuret J, Arch Biochem Biophys. 2001 Mar 1;387(1):11-9. PMID:11368172
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