1k28: Difference between revisions

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<StructureSection load='1k28' size='340' side='right'caption='[[1k28]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='1k28' size='340' side='right'caption='[[1k28]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1k28]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K28 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1K28 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1k28]] is a 2 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=1K28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K28 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.9&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4]), 27 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</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=1k28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k28 OCA], [https://pdbe.org/1k28 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k28 RCSB], [https://www.ebi.ac.uk/pdbsum/1k28 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k28 ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1k28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k28 OCA], [http://pdbe.org/1k28 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1k28 RCSB], [http://www.ebi.ac.uk/pdbsum/1k28 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1k28 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/VG05_BPT4 VG05_BPT4]] Tail-associated lysozyme 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. [[http://www.uniprot.org/uniprot/VG27_BPT4 VG27_BPT4]] Structural component of the baseplate.
[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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1k28 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1k28 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacteriophage T4 has a very efficient mechanism for infecting cells. The key component of this process is the baseplate, located at the end of the phage tail, which regulates the interaction of the tail fibres and the DNA ejection machine. A complex of gene product (gp) 5 (63K) and gp27 (44K), the central part of the baseplate, is required to penetrate the outer cell membrane of Escherichia coli and to disrupt the intermembrane peptidoglycan layer, promoting subsequent entry of phage DNA into the host. We present here a crystal structure of the (gp5-gp27)3 321K complex, determined to 2.9 A resolution and fitted into a cryo-electron microscopy map at 17 A resolution of the baseplate-tail tube assembly. The carboxy-terminal domain of gp5 is a triple-stranded beta-helix that forms an equilateral triangular prism, which acts as a membrane-puncturing needle. The middle lysozyme domain of gp5, situated on the periphery of the prism, serves to digest the peptidoglycan layer. The amino-terminal, antiparallel beta-barrel domain of gp5 is inserted into a cylinder formed by three gp27 monomers, which may serve as a channel for DNA ejection.
Structure of the cell-puncturing device of bacteriophage T4.,Kanamaru S, Leiman PG, Kostyuchenko VA, Chipman PR, Mesyanzhinov VV, Arisaka F, Rossmann MG Nature. 2002 Jan 31;415(6871):553-7. PMID:11823865<ref>PMID:11823865</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1k28" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bpt4]]
[[Category: Escherichia virus T4]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lysozyme]]
[[Category: Arisaka F]]
[[Category: Arisaka, F]]
[[Category: Chipman PR]]
[[Category: Chipman, P R]]
[[Category: Kanamaru S]]
[[Category: Kanamaru, S]]
[[Category: Kostyuchenko VA]]
[[Category: Kostyuchenko, V A]]
[[Category: Leiman PG]]
[[Category: Leiman, P G]]
[[Category: Mesyanzhinov VV]]
[[Category: Mesyanzhinov, V V]]
[[Category: Rossmann MG]]
[[Category: Rossmann, M G]]
[[Category: Gp27-gp5*-gp5c]]
[[Category: Hub]]
[[Category: Hydrolase-structural protein complex]]
[[Category: Ob fold]]
[[Category: Pseudohexamer]]
[[Category: T4 tail lysozyme]]
[[Category: Triple-stranded beta-helix]]

Revision as of 10:57, 3 April 2024

The Structure of the Bacteriophage T4 Cell-Puncturing DeviceThe Structure of the Bacteriophage T4 Cell-Puncturing Device

Structural highlights

1k28 is a 2 chain structure with sequence from Escherichia virus T4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Weigele PR, Scanlon E, King J. Homotrimeric, beta-stranded viral adhesins and tail proteins. J Bacteriol. 2003 Jul;185(14):4022-30. PMID:12837775
  2. ↑ Leiman PG, Arisaka F, van Raaij MJ, Kostyuchenko VA, Aksyuk AA, Kanamaru S, Rossmann MG. Morphogenesis of the T4 tail and tail fibers. Virol J. 2010 Dec 3;7:355. doi: 10.1186/1743-422X-7-355. PMID:21129200 doi:10.1186/1743-422X-7-355

1k28, resolution 2.90Å

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