1wvl
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(New page: 200px<br /><applet load="1wvl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wvl, resolution 2.6Å" /> '''Crystal Structure of ...)
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Revision as of 03:35, 21 November 2007
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Crystal Structure of Multimeric DNA-binding Protein Sac7d-GCN4 with DNA decamer
Overview
The protein Sac7d belongs to a class of small chromosomal proteins from, the hyperthermophilic archaeon Sulfolobus acidocaldarius. Sac7d is, extremely stable to heat, acid, and chemical agents. This protein is a, monomer and it binds DNA without any particular sequence preference, while, inducing a sharp kink in the DNA. By appending a leucine-zipper-like, helical peptide derived from the yeast transcriptional activator GCN4 to, the C-terminal end of Sac7d, the modified monomers (denoted S7dLZ) are, expected to interact with each other via hydrophobic force to form a, parallel dimer. The recombinant S7dLZ was expressed in Escherichia coli, and purified by heating and ion-exchange chromatography. The formation of, dimer was detected by gel-filtration chromatography and chemical, cross-link. The results of surface plasmon resonance and circular, dichroism experiments showed that the DNA-binding capacity was retained., Furthermore, X-ray diffraction analysis of single crystals of S7dLZ in, complex with DNA decamer CCTATATAGG showed that the leucine-zipper, segments of S7dLZ were associated into an antiparallel four-helix bundle., There are two DNA fragments bound to each S7dLZ tetramer in the crystal., This model works as a successful template that endows protein a new, function without losing original properties.
About this Structure
1WVL is a Single protein structure of sequence from Sulfolobus acidocaldarius. Full crystallographic information is available from OCA.
Reference
Design and characterization of a multimeric DNA binding protein using Sac7d and GCN4 as templates., Wu SW, Ko TP, Chou CC, Wang AH, Proteins. 2005 Sep 1;60(4):617-28. PMID:16028219
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