We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

6bl5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (14:22, 13 March 2024) (edit) (undo)
 
Line 1: Line 1:
==Head decoration protein from the hyperthermophilic phage P74-26==
==Head decoration protein from the hyperthermophilic phage P74-26==
-
<StructureSection load='6bl5' size='340' side='right' caption='[[6bl5]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
+
<StructureSection load='6bl5' size='340' side='right'caption='[[6bl5]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6bl5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_phage_p74-26 Thermus phage p74-26]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BL5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BL5 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6bl5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_virus_P74-26 Thermus virus P74-26]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BL5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BL5 FirstGlance]. <br>
-
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">P74p87 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=466052 Thermus phage P74-26])</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]] 1.69&#8491;</td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6bl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bl5 OCA], [http://pdbe.org/6bl5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bl5 RCSB], [http://www.ebi.ac.uk/pdbsum/6bl5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bl5 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=6bl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bl5 OCA], [https://pdbe.org/6bl5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bl5 RCSB], [https://www.ebi.ac.uk/pdbsum/6bl5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bl5 ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/A7XXR5_BP742 A7XXR5_BP742]
-
Virus capsids are protein shells that protect the viral genome from environmental assaults, while maintaining the high internal pressure of the tightly packaged genome. To elucidate how capsids maintain stability under harsh conditions, we investigated the capsid components of the hyperthermophilic phage P74-26. We determined the structure of capsid protein gp87 and show that it has the same fold as decoration proteins in many other phages, despite lacking significant sequence homology. We also find that gp87 is significantly more stable than mesophilic homologs. Our analysis of the gp87 structure reveals that the core "beta tulip" domain is conserved in trimeric capsid components across numerous double-stranded DNA viruses, including Herpesviruses. Moreover, this beta barrel domain is found in anti-CRISPR protein AcrIIC1, suggesting a mechanism for the evolution of this Cas9 inhibitor. Our work illustrates the principles for increased stability of gp87, and extends the evolutionary reach of the beta tulip domain.
+
-
 
+
-
A Hyperthermophilic Phage Decoration Protein Suggests Common Evolutionary Origin with Herpesvirus Triplex Proteins and an Anti-CRISPR Protein.,Stone NP, Hilbert BJ, Hidalgo D, Halloran KT, Lee J, Sontheimer EJ, Kelch BA Structure. 2018 Apr 26. pii: S0969-2126(18)30133-3. doi:, 10.1016/j.str.2018.04.008. PMID:29779790<ref>PMID:29779790</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 6bl5" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Thermus phage p74-26]]
+
[[Category: Large Structures]]
-
[[Category: Halloran, K T]]
+
[[Category: Thermus virus P74-26]]
-
[[Category: Hidalgo, D]]
+
[[Category: Halloran KT]]
-
[[Category: Hilbert, B J]]
+
[[Category: Hidalgo D]]
-
[[Category: Kelch, B A]]
+
[[Category: Hilbert BJ]]
-
[[Category: Stone, N P]]
+
[[Category: Kelch BA]]
-
[[Category: Beta-tulip domain]]
+
[[Category: Stone NP]]
-
[[Category: Capsid]]
+
-
[[Category: Viral protein]]
+
-
[[Category: Virion]]
+

Current revision

Head decoration protein from the hyperthermophilic phage P74-26

PDB ID 6bl5

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6bl5"
Personal tools