1hyw

From Proteopedia

(Difference between revisions)

Current revision

SOLUTION STRUCTURE OF BACTERIOPHAGE LAMBDA GPW

Structural highlights

1hyw is a 1 chain structure with sequence from Escherichia virus Lambda. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HCP_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 PubMed

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.

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

↑ Murialdo H, Xing X, Tzamtzis D, Haddad A, Gold M. The product of the bacteriophage lambda W gene: purification and properties. Biochem Cell Biol. 2003 Aug;81(4):307-15. doi: 10.1139/o03-059. PMID:14569303 doi:http://dx.doi.org/10.1139/o03-059
↑ Cardarelli L, Pell LG, Neudecker P, Pirani N, Liu A, Baker LA, Rubinstein JL, Maxwell KL, Davidson AR. Phages have adapted the same protein fold to fulfill multiple functions in virion assembly. Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14384-9. Epub 2010 Jul 26. PMID:20660769
↑ Casjens S, Horn T, Kaiser AD. Head assembly steps controlled by genes F and W in bacteriophage lambda. J Mol Biol. 1972 Mar 14;64(3):551-63. PMID:5022189
↑ Maxwell KL, Yee AA, Booth V, Arrowsmith CH, Gold M, Davidson AR. The solution structure of bacteriophage lambda protein W, a small morphogenetic protein possessing a novel fold. J Mol Biol. 2001 Apr 20;308(1):9-14. PMID:11302702 doi:http://dx.doi.org/10.1006/jmbi.2001.4582

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hyw"

@@ Line 1: / Line 1: @@
 ==SOLUTION STRUCTURE OF BACTERIOPHAGE LAMBDA GPW==
-<StructureSection load='1hyw' size='340' side='right'caption='[[1hyw]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
+<StructureSection load='1hyw' size='340' side='right'caption='[[1hyw]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hyw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteriophage_lambda Bacteriophage lambda]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HYW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hyw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Lambda Escherichia virus Lambda]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HYW FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10710 Bacteriophage lambda])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hyw OCA], [https://pdbe.org/1hyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hyw RCSB], [https://www.ebi.ac.uk/pdbsum/1hyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hyw ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/VHTJ_LAMBD VHTJ_LAMBD]] Required for the stabilization of DNA within the phage head and for attachment of tails onto the head during morphogenesis.
+[https://www.uniprot.org/uniprot/HCP_LAMBD HCP_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.<ref>PMID:14569303</ref> <ref>PMID:20660769</ref> <ref>PMID:5022189</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Bacteriophage lambda]]
+[[Category: Escherichia virus Lambda]]
 [[Category: Large Structures]]
-[[Category: Arrowsmith, C H]]
+[[Category: Arrowsmith CH]]
-[[Category: Booth, V]]
+[[Category: Booth V]]
-[[Category: Davidson, A R]]
+[[Category: Davidson AR]]
-[[Category: Gold, M]]
+[[Category: Gold M]]
-[[Category: Maxwell, K L]]
+[[Category: Maxwell KL]]
-[[Category: Yee, A A]]
+[[Category: Yee AA]]
-[[Category: Novel fold]]
-[[Category: One two-stranded beta-sheet]]
-[[Category: Two helice]]
-[[Category: Viral protein]]

1hyw

From Proteopedia

Current revision

SOLUTION STRUCTURE OF BACTERIOPHAGE LAMBDA GPW

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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