1hyw
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(New page: 200px<br /><applet load="1hyw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hyw" /> '''SOLUTION STRUCTURE OF BACTERIOPHAGE LAMBDA G...)
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Revision as of 14:48, 20 November 2007
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SOLUTION STRUCTURE OF BACTERIOPHAGE LAMBDA GPW
Overview
Protein W (gpW) from bacteriophage lambda is required for the, stabilization of DNA within the phage head and for attachment of tails, onto the head during morphogenesis. Although comprised of only 68, residues, it likely interacts with at least two other proteins in the, mature phage and with DNA. Thus, gpW is an intriguing subject for detailed, structural studies. We have determined its solution structure using NMR, spectroscopy and have found it to possesses a novel fold consisting of two, alpha-helices and a single two-stranded beta-sheet arranged around a, well-packed hydrophobic core. The 14 C-terminal residues of gpW, which are, essential for function, are unstructured in solution.
About this Structure
1HYW is a Single protein structure of sequence from Enterobacteria phage lambda. Full crystallographic information is available from OCA.
Reference
The solution structure of bacteriophage lambda protein W, a small morphogenetic protein possessing a novel fold., Maxwell KL, Yee AA, Booth V, Arrowsmith CH, Gold M, Davidson AR, J Mol Biol. 2001 Apr 20;308(1):9-14. PMID:11302702
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