Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein.

doi:10.1021/bi800204k

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Article

Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein.

Biochemistry - 1 Jul 2008

Meinke Gretchen, Ezeokonkwo Chukwudi, Balbo Paul, Stafford Walter, Moore Claire, Bohm Andrew

Abstract excerpt

In yeast, the mRNA processing enzyme poly(A) polymerase is tethered to the much larger 3'-end processing complex via Fip1, a 36 kDa protein of unknown structure. We report the 2.6 A crystal structure of yeast poly(A) polymerase in complex with a peptide containing residues 80-105 of Fip1. The Fip1 peptide binds to the outside surface of the C-terminal domain of the polymerase. On the basis of this structure, we...

Topics

Amino Acid Sequence
Biophysical Phenomena
Biophysics
Conserved Sequence
Crystallography, X-Ray
Humans
Kinetics
Models, Molecular
Molecular Sequence Data
Mutation
Pancreatitis-Associated Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Peptides

Polynucleotide Adenylyltransferase

Protein Binding

Protein Structure, Quaternary

Saccharomyces cerevisiae

Saccharomyces cerevisiae Proteins

Sequence Alignment

Source

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Identifiers

PMID: 18537269
DOI: 10.1021/bi800204k
PMCID: PMC2615413

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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