1ajy

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1ajy

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STRUCTURE AND MOBILITY OF THE PUT3 DIMER: A DNA PINCER, NMR, 13 STRUCTURES

Overview

The solution structure and backbone dynamics of the transcriptional, activator PUT3 (31-100) has been characterized using NMR spectroscopy., PUT3 (31-100) contains three distinct domains: a cysteine zinc cluster, linker, and dimerization domain. The cysteine zinc cluster of PUT3 closely, resembles the solution structure of GAL4, while the dimerization domain, forms a long coiled-coil similar to that observed in the crystal, structures of GAL4 and PPR1. However, the residues at the N-terminal end, of the coiled-coil behave very differently in each of these proteins. A, comparison of the structural elements within this region provides a model, for the DNA binding specificity of these proteins. Furthermore, we have, characterized the dynamics of PUT3 to find that the zinc cluster and, dimerization domains have very diverse dynamics in solution. The, dimerization domain behaves as a large protein, while the peripheral, cysteine zinc clusters have dynamic properties similar to small proteins.

About this Structure

1AJY is a Single protein structure of sequence from Saccharomyces cerevisiae with ZN as ligand. Full crystallographic information is available from OCA.

Reference

Structure and mobility of the PUT3 dimer., Walters KJ, Dayie KT, Reece RJ, Ptashne M, Wagner G, Nat Struct Biol. 1997 Sep;4(9):744-50. PMID:9303003

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