4jj2
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4jj2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JJ2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4jj2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JJ2 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ELA:9-OCTADECENOIC+ACID'>ELA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=STE:STEARIC+ACID'>STE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.28Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ELA:9-OCTADECENOIC+ACID'>ELA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=STE:STEARIC+ACID'>STE</scene></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=4jj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jj2 OCA], [https://pdbe.org/4jj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jj2 RCSB], [https://www.ebi.ac.uk/pdbsum/4jj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jj2 ProSAT]</span></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=4jj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jj2 OCA], [https://pdbe.org/4jj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jj2 RCSB], [https://www.ebi.ac.uk/pdbsum/4jj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jj2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/NEEDL_BPT4 NEEDL_BPT4] Tail-associated lysozyme of the baseplate hub that is essential for localized hydrolysis of bacterial cell wall necessary for viral DNA injection. The needle-like gp5 protein punctures the outer cell membrane and then digests the peptidoglycan cell wall in the periplasmic space. Involved in the tail assembly.<ref>PMID:12837775</ref> <ref>PMID:21129200</ref> | [https://www.uniprot.org/uniprot/NEEDL_BPT4 NEEDL_BPT4] Tail-associated lysozyme of the baseplate hub that is essential for localized hydrolysis of bacterial cell wall necessary for viral DNA injection. The needle-like gp5 protein punctures the outer cell membrane and then digests the peptidoglycan cell wall in the periplasmic space. Involved in the tail assembly.<ref>PMID:12837775</ref> <ref>PMID:21129200</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Gene product 5 (gp5) of bacteriophage T4 is a spike-shaped protein that functions to disrupt the membrane of the target cell during phage infection. Its C-terminal domain is a long and slender beta-helix that is formed by three polypeptide chains wrapped around a common symmetry axis akin to three interdigitated corkscrews. The folding and biophysical properties of such triple-stranded beta-helices, which are topologically related to amyloid fibers, represent an unsolved biophysical problem. Here, we report structural and biophysical characterization of T4 gp5 beta-helix and its truncated mutants of different lengths. A soluble fragment that forms a dimer of trimers and that could comprise a minimal self-folding unit has been identified. Surprisingly, the hydrophobic core of the beta-helix is small. It is located near the C-terminal end of the beta-helix and contains a centrally positioned and hydrated magnesium ion. A large part of the beta-helix interior comprises a large elongated cavity that binds palmitic, stearic, and oleic acids in an extended conformation suggesting that these molecules might participate in the folding of the complete beta-helix. | ||
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| + | Structure and Biophysical Properties of a Triple-Stranded Beta-Helix Comprising the Central Spike of Bacteriophage T4.,Buth SA, Menin L, Shneider MM, Engel J, Boudko SP, Leiman PG Viruses. 2015 Aug 18;7(8):4676-706. doi: 10.3390/v7082839. PMID:26295253<ref>PMID:26295253</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4jj2" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
High resolution structure of a C-terminal fragment of the T4 phage gp5 beta-helix
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