2npi
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(New page: 200px<br /><applet load="2npi" size="450" color="white" frame="true" align="right" spinBox="true" caption="2npi, resolution 2.95Å" /> '''Clp1-ATP-Pcf11 compl...)
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Revision as of 10:42, 21 November 2007
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Clp1-ATP-Pcf11 complex
Overview
Pcf11 and Clp1 are subunits of cleavage factor IA (CFIA), an essential, polyadenylation factor in Saccahromyces cerevisiae. We have determined the, structure of a ternary complex of Clp1 together with ATP and the, Clp1-binding region of Pcf11. Clp1 contains three domains, a small, N-terminal beta sandwich domain, a C-terminal domain containing a novel, alpha/beta-fold and a central domain that binds ATP. The arrangement of, the nucleotide binding site is similar to that observed in SIMIBI-class, ATPase subunits found in other multisubunit macromolecular complexes., However, despite this similarity, nucleotide hydrolysis does not occur., The Pcf11 binding site is also located in the central domain where three, highly conserved residues in Pcf11 mediate many of the protein-protein, interactions. We propose that this conserved Clp1-Pcf11 interaction is, responsible for maintaining a tight coupling between the Clp1 nucleotide, binding subunit and the other components of the polyadenylation machinery., Moreover, we suggest that this complex represents a stabilized ATP bound, form of Clp1 that requires the participation of other non-CFIA processing, factors in order to initiate timely ATP hydrolysis during 3' end, processing.
About this Structure
2NPI is a Protein complex structure of sequences from Saccharomyces cerevisiae with MG and ATP as ligands. Full crystallographic information is available from OCA.
Reference
Structure of a nucleotide-bound Clp1-Pcf11 polyadenylation factor., Noble CG, Beuth B, Taylor IA, Nucleic Acids Res. 2007;35(1):87-99. Epub 2006 Dec 6. PMID:17151076
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