5iw9

From Proteopedia

(Difference between revisions)

Current revision

Structure of bacteriophage T4 gp25, sheath polymerization initiator

Structural highlights

5iw9 is a 2 chain structure with sequence from Escherichia virus T4. This structure supersedes the now removed PDB entry 4hrz. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.47Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BP25_BPT4 Baseplate protein that is part of the outer wedges of the baseplate (PubMed:15315755). Probably plays a role as a connector between the central and peripheral parts of the baseplate. Involved in the tail assembly.[UniProtKB:P51768]^[1] ^[2]

Publication Abstract from PubMed

Several systems, including contractile tail bacteriophages, the type VI secretion system and R-type pyocins, use a multiprotein tubular apparatus to attach to and penetrate host cell membranes. This macromolecular machine resembles a stretched, coiled spring (or sheath) wound around a rigid tube with a spike-shaped protein at its tip. A baseplate structure, which is arguably the most complex part of this assembly, relays the contraction signal to the sheath. Here we present the atomic structure of the approximately 6-megadalton bacteriophage T4 baseplate in its pre- and post-host attachment states and explain the events that lead to sheath contraction in atomic detail. We establish the identity and function of a minimal set of components that is conserved in all contractile injection systems and show that the triggering mechanism is universally conserved.

Structure of the T4 baseplate and its function in triggering sheath contraction.,Taylor NM, Prokhorov NS, Guerrero-Ferreira RC, Shneider MM, Browning C, Goldie KN, Stahlberg H, Leiman PG Nature. 2016 May 18;533(7603):346-52. doi: 10.1038/nature17971. PMID:27193680^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Leiman PG, Chipman PR, Kostyuchenko VA, Mesyanzhinov VV, Rossmann MG. Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host. Cell. 2004 Aug 20;118(4):419-29. PMID:15315755 doi:10.1016/j.cell.2004.07.022
↑ 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
↑ Taylor NM, Prokhorov NS, Guerrero-Ferreira RC, Shneider MM, Browning C, Goldie KN, Stahlberg H, Leiman PG. Structure of the T4 baseplate and its function in triggering sheath contraction. Nature. 2016 May 18;533(7603):346-52. doi: 10.1038/nature17971. PMID:27193680 doi:http://dx.doi.org/10.1038/nature17971

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/5iw9"

Categories: Escherichia virus T4 | Large Structures | Browning C | Leiman PG | Shneider MM

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5iw9 is ON HOLD
+==Structure of bacteriophage T4 gp25, sheath polymerization initiator==
+<StructureSection load='5iw9' size='340' side='right'caption='[[5iw9]], [[Resolution|resolution]] 2.47&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5iw9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4hrz 4hrz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IW9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IW9 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.47&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5iw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iw9 OCA], [https://pdbe.org/5iw9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iw9 RCSB], [https://www.ebi.ac.uk/pdbsum/5iw9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iw9 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/BP25_BPT4 BP25_BPT4] Baseplate protein that is part of the outer wedges of the baseplate (PubMed:15315755). Probably plays a role as a connector between the central and peripheral parts of the baseplate. Involved in the tail assembly.[UniProtKB:P51768]<ref>PMID:15315755</ref> <ref>PMID:21129200</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Several systems, including contractile tail bacteriophages, the type VI secretion system and R-type pyocins, use a multiprotein tubular apparatus to attach to and penetrate host cell membranes. This macromolecular machine resembles a stretched, coiled spring (or sheath) wound around a rigid tube with a spike-shaped protein at its tip. A baseplate structure, which is arguably the most complex part of this assembly, relays the contraction signal to the sheath. Here we present the atomic structure of the approximately 6-megadalton bacteriophage T4 baseplate in its pre- and post-host attachment states and explain the events that lead to sheath contraction in atomic detail. We establish the identity and function of a minimal set of components that is conserved in all contractile injection systems and show that the triggering mechanism is universally conserved.
-Authors: Leiman, P.G., Browning, C., Shneider, M.M.
+Structure of the T4 baseplate and its function in triggering sheath contraction.,Taylor NM, Prokhorov NS, Guerrero-Ferreira RC, Shneider MM, Browning C, Goldie KN, Stahlberg H, Leiman PG Nature. 2016 May 18;533(7603):346-52. doi: 10.1038/nature17971. PMID:27193680<ref>PMID:27193680</ref>
-Description: Structure of bacteriophage T4 gp25, sheath polymerization initiator
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Browning, C]]
+<div class="pdbe-citations 5iw9" style="background-color:#fffaf0;"></div>
-[[Category: Leiman, P.G]]
+== References ==
-[[Category: Shneider, M.M]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia virus T4]]
+[[Category: Large Structures]]
+[[Category: Browning C]]
+[[Category: Leiman PG]]
+[[Category: Shneider MM]]

5iw9

From Proteopedia

Current revision

Structure of bacteriophage T4 gp25, sheath polymerization initiator

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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