5hx2
From Proteopedia
(Difference between revisions)
| Line 8: | Line 8: | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/BP53_BPT4 BP53_BPT4]] Baseplate protein that is part of the baseplate wedge (PubMed:15315755). Involved in the tail assembly.<ref>PMID:15315755</ref> <ref>PMID:21129200</ref> [[http://www.uniprot.org/uniprot/BP07_BPT4 BP07_BPT4]] Baseplate protein that is part of the baseplate wedge. Involved in the tail assembly.<ref>PMID:2254933</ref> <ref>PMID:21129200</ref> [[http://www.uniprot.org/uniprot/BP06_BPT4 BP06_BPT4]] Baseplate protein that is part of the baseplate wedge (PubMed:15315755). Involved in the tail assembly.<ref>PMID:15315755</ref> <ref>PMID:21129200</ref> [[http://www.uniprot.org/uniprot/BP08_BPT4 BP08_BPT4]] Baseplate protein that is part of the baseplate wedge. Involved in the tail assembly.<ref>PMID:15315755</ref> <ref>PMID:21129200</ref> [[http://www.uniprot.org/uniprot/BP10_BPT4 BP10_BPT4]] Baseplate protein that is part of the baseplate wedge and that connects the short tail fibers to the baseplate (PubMed:16554069). During infection, the baseplate undergoes a conformational change from a dome-shaped to a star-shaped structure. At this point, gp10 rotates and acts as a lever that unfolds the short tail fibers, which then interact with host cell surface receptors. Involved in the tail assembly.<ref>PMID:16554069</ref> <ref>PMID:21129200</ref> | [[http://www.uniprot.org/uniprot/BP53_BPT4 BP53_BPT4]] Baseplate protein that is part of the baseplate wedge (PubMed:15315755). Involved in the tail assembly.<ref>PMID:15315755</ref> <ref>PMID:21129200</ref> [[http://www.uniprot.org/uniprot/BP07_BPT4 BP07_BPT4]] Baseplate protein that is part of the baseplate wedge. Involved in the tail assembly.<ref>PMID:2254933</ref> <ref>PMID:21129200</ref> [[http://www.uniprot.org/uniprot/BP06_BPT4 BP06_BPT4]] Baseplate protein that is part of the baseplate wedge (PubMed:15315755). Involved in the tail assembly.<ref>PMID:15315755</ref> <ref>PMID:21129200</ref> [[http://www.uniprot.org/uniprot/BP08_BPT4 BP08_BPT4]] Baseplate protein that is part of the baseplate wedge. Involved in the tail assembly.<ref>PMID:15315755</ref> <ref>PMID:21129200</ref> [[http://www.uniprot.org/uniprot/BP10_BPT4 BP10_BPT4]] Baseplate protein that is part of the baseplate wedge and that connects the short tail fibers to the baseplate (PubMed:16554069). During infection, the baseplate undergoes a conformational change from a dome-shaped to a star-shaped structure. At this point, gp10 rotates and acts as a lever that unfolds the short tail fibers, which then interact with host cell surface receptors. Involved in the tail assembly.<ref>PMID:16554069</ref> <ref>PMID:21129200</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacteriophage T4 consists of a head for protecting its genome and a sheathed tail for inserting its genome into a host. The tail terminates with a multiprotein baseplate that changes its conformation from a "high-energy" dome-shaped to a "low-energy" star-shaped structure during infection. Although these two structures represent different minima in the total energy landscape of the baseplate assembly, as the dome-shaped structure readily changes to the star-shaped structure when the virus infects a host bacterium, the dome-shaped structure must have more energy than the star-shaped structure. Here we describe the electron microscopy structure of a 3.3-MDa in vitro-assembled star-shaped baseplate with a resolution of 3.8 A. This structure, together with other genetic and structural data, shows why the high-energy baseplate is formed in the presence of the central hub and how the baseplate changes to the low-energy structure, via two steps during infection. Thus, the presence of the central hub is required to initiate the assembly of metastable, high-energy structures. If the high-energy structure is formed and stabilized faster than the low-energy structure, there will be insufficient components to assemble the low-energy structure. | ||
| + | |||
| + | Role of bacteriophage T4 baseplate in regulating assembly and infection.,Yap ML, Klose T, Arisaka F, Speir JA, Veesler D, Fokine A, Rossmann MG Proc Natl Acad Sci U S A. 2016 Mar 8;113(10):2654-9. doi:, 10.1073/pnas.1601654113. Epub 2016 Feb 29. PMID:26929357<ref>PMID:26929357</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5hx2" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 17:03, 10 May 2016
In vitro assembled star-shaped hubless T4 baseplate
| |||||||||||
Categories: Fokine, A | Klose, T | Rossmann, M G | Yap, M L | Baseplate | Complex | T4 | Viral protein
