1hyw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(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...)
Line 1: Line 1:
-
[[Image:1hyw.gif|left|200px]]<br /><applet load="1hyw" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1hyw.gif|left|200px]]<br /><applet load="1hyw" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1hyw" />
caption="1hyw" />
'''SOLUTION STRUCTURE OF BACTERIOPHAGE LAMBDA GPW'''<br />
'''SOLUTION STRUCTURE OF BACTERIOPHAGE LAMBDA GPW'''<br />
==Overview==
==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.
+
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==
==About this Structure==
-
1HYW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_lambda Enterobacteria phage lambda]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HYW OCA].
+
1HYW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_lambda Enterobacteria phage lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HYW OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Enterobacteria phage lambda]]
[[Category: Enterobacteria phage lambda]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Arrowsmith, C.H.]]
+
[[Category: Arrowsmith, C H.]]
[[Category: Booth, V.]]
[[Category: Booth, V.]]
-
[[Category: Davidson, A.R.]]
+
[[Category: Davidson, A R.]]
[[Category: Gold, M.]]
[[Category: Gold, M.]]
-
[[Category: Maxwell, K.L.]]
+
[[Category: Maxwell, K L.]]
-
[[Category: Yee, A.A.]]
+
[[Category: Yee, A A.]]
[[Category: novel fold; two helices]]
[[Category: novel fold; two helices]]
[[Category: one two-stranded beta-sheet]]
[[Category: one two-stranded beta-sheet]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:55:15 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:14 2008''

Revision as of 11:06, 21 February 2008


1hyw

Drag the structure with the mouse to rotate

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

Page seeded by OCA on Thu Feb 21 13:06:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools