1HYW

SOLUTION STRUCTURE OF BACTERIOPHAGE LAMBDA GPW

Summary for 1HYW

• Entry DOI: 10.2210/pdb1hyw/pdb
• Descriptor: HEAD-TO-TAIL JOINING PROTEIN W (1 entity in total)
• Functional Keywords: novel fold; two helices, one two-stranded beta-sheet, viral protein
• Biological source: Enterobacteria phage lambda
• Total number of polymer chains: 1
• Total formula weight: 7625.75

Authors

Maxwell, K.L.,Yee, A.A.,Booth, V.,Arrowsmith, C.H.,Gold, M.,Davidson, A.R. (deposition date: 2001-01-22, release date: 2001-04-25, Last modification date: 2024-05-29)

Primary citation

Maxwell, K.L.,Yee, A.A.,Booth, V.,Arrowsmith, C.H.,Gold, M.,Davidson, A.R.
The solution structure of bacteriophage lambda protein W, a small morphogenetic protein possessing a novel fold.
J.Mol.Biol., 308:9-14, 2001

PubMed Abstract: 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.

PubMed: 11302702
DOI: 10.1006/jmbi.2001.4582

Experimental method

SOLUTION NMR