1hyw
From Proteopedia
SOLUTION STRUCTURE OF BACTERIOPHAGE LAMBDA GPW
Structural highlights
FunctionHCP_LAMBD Plays a role in morphogenesis of the virion head after genome packaging. Presumably interacts with the portal vertex to stabilize the packaged DNA within the head after packaging. Probably binds to the head-tail connector protein FII.[1] [2] [3] Publication Abstract from PubMedProtein 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. 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||
