1wvl
From Proteopedia
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[[Image:1wvl.gif|left|200px]] | [[Image:1wvl.gif|left|200px]] | ||
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'''Crystal Structure of Multimeric DNA-binding Protein Sac7d-GCN4 with DNA decamer''' | '''Crystal Structure of Multimeric DNA-binding Protein Sac7d-GCN4 with DNA decamer''' | ||
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[[Category: Wang, A H.]] | [[Category: Wang, A H.]] | ||
[[Category: Wu, S W.]] | [[Category: Wu, S W.]] | ||
- | [[Category: | + | [[Category: Leucine zipper]] |
- | [[Category: | + | [[Category: Protein engineering]] |
- | [[Category: | + | [[Category: Synchrotron radiation]] |
- | [[Category: | + | [[Category: Thermophile]] |
- | [[Category: | + | [[Category: X-ray crystallography]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:11:43 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 11:11, 3 May 2008
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 Page seeded by OCA on Sat May 3 14:11:43 2008