6n4v
From Proteopedia
(Difference between revisions)
| (One intermediate revision not shown.) | |||
| Line 3: | Line 3: | ||
<SX load='6n4v' size='340' side='right' viewer='molstar' caption='[[6n4v]], [[Resolution|resolution]] 3.00Å' scene=''> | <SX load='6n4v' size='340' side='right' viewer='molstar' caption='[[6n4v]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6n4v]] is a 120 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[6n4v]] is a 120 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_phage_PP7 Pseudomonas phage PP7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N4V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N4V FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3Å</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=6n4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n4v OCA], [https://pdbe.org/6n4v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n4v RCSB], [https://www.ebi.ac.uk/pdbsum/6n4v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n4v ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CAPSD_BPPP7 CAPSD_BPPP7] Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins) (PubMed:10739912). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome (By similarity).[UniProtKB:P03612]<ref>PMID:10739912</ref> Acts as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site.<ref>PMID:11306589</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 15: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 6n4v" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6n4v" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</SX> | </SX> | ||
| - | [[Category: Bppp7]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Carragher | + | [[Category: Pseudomonas phage PP7]] |
| - | [[Category: Finn | + | [[Category: Carragher B]] |
| - | [[Category: Kopylov | + | [[Category: Finn MG]] |
| - | [[Category: Liangjun | + | [[Category: Kopylov M]] |
| - | [[Category: Potter | + | [[Category: Liangjun Z]] |
| - | + | [[Category: Potter CS]] | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
CryoEM structure of Leviviridae PP7 WT coat protein dimer capsid (PP7PP7-WT)
| |||||||||
