6ui6

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Current revision (14:57, 13 March 2024) (edit) (undo)
 
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<SX load='6ui6' size='340' side='right' viewer='molstar' caption='[[6ui6]], [[Resolution|resolution]] 3.53&Aring;' scene=''>
<SX load='6ui6' size='340' side='right' viewer='molstar' caption='[[6ui6]], [[Resolution|resolution]] 3.53&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6ui6]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Hbv Hbv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UI6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6UI6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6ui6]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Hepatitis_B_virus Hepatitis B virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UI6 FirstGlance]. <br>
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</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=6ui6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ui6 OCA], [http://pdbe.org/6ui6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ui6 RCSB], [http://www.ebi.ac.uk/pdbsum/6ui6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ui6 ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.53&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ui6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ui6 OCA], [https://pdbe.org/6ui6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ui6 RCSB], [https://www.ebi.ac.uk/pdbsum/6ui6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ui6 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/CAPSD_HBVA2 CAPSD_HBVA2] Self assembles to form an icosahedral capsid. Most capsids appear to be large particles with an icosahedral symmetry of T=4 and consist of 240 copies of capsid protein, though a fraction forms smaller T=3 particles consisting of 180 capsid proteins. Entering capsids are transported along microtubules to the nucleus. Phosphorylation of the capsid is thought to induce exposure of nuclear localization signal in the C-terminal portion of the capsid protein that allows binding to the nuclear pore complex via the importin (karyopherin-) alpha and beta. Capsids are imported in intact form through the nuclear pore into the nuclear basket, where it probably binds NUP153. Only capsids that contain the mature viral genome can release the viral DNA and capsid protein into the nucleoplasm. Immature capsids get stuck in the basket. Capsids encapsulate the pre-genomic RNA and the P protein. Pre-genomic RNA is reverse-transcribed into DNA while the capsid is still in the cytoplasm. The capsid can then either be directed to the nucleus, providing more genomes for transcription, or bud through the endoplasmic reticulum to provide new virions.[HAMAP-Rule:MF_04076]
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Hepatitis B virus (HBV) is a leading cause of liver disease. The capsid is an essential component of the virion and it is therefore of interest how it assembles and disassembles. The capsid protein is unusual both for its rare fold and that it polymerizes according to two different icosahedral symmetries, causing the polypeptide chain to exist in seven quasi-equivalent environments: A, B, and C in AB and CC dimers in T = 3 capsids, and A, B, C, and D in AB and CD dimers in T = 4 capsids. We have compared the two capsids by cryo-EM at 3.5 A resolution. To ensure a valid comparison, the two capsids were prepared and imaged under identical conditions. We find that the chains have different conformations and potential energies, with the T = 3 C chain having the lowest. Three of the four quasi-equivalent dimers are asymmetric with respect to conformation and potential energy; however, the T = 3 CC dimer is symmetrical and has the lowest potential energy although its intra-dimer interface has the least free energy of formation. Of all the inter-dimer interfaces, the CB interface has the least area and free energy, in both capsids. From the calculated energies of higher-order groupings of dimers discernible in the lattices we predict early assembly intermediates, and indeed we observe such structures by negative stain EM of in vitro assembly reactions. By sequence analysis and computational alanine scanning we identify key residues and motifs involved in capsid assembly. Our results explain several previously reported observations on capsid assembly, disassembly, and dimorphism.
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Expression of quasi-equivalence and capsid dimorphism in the Hepadnaviridae.,Wu W, Watts NR, Cheng N, Huang R, Steven AC, Wingfield PT PLoS Comput Biol. 2020 Apr 20;16(4):e1007782. doi: 10.1371/journal.pcbi.1007782. , eCollection 2020 Apr. PMID:32310951<ref>PMID:32310951</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6ui6" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
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[[Category: Hbv]]
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[[Category: Hepatitis B virus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cheng, N]]
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[[Category: Cheng N]]
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[[Category: Huang, R]]
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[[Category: Huang R]]
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[[Category: Steven, A]]
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[[Category: Steven A]]
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[[Category: Watts, N R]]
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[[Category: Watts NR]]
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[[Category: Wingfield, P T]]
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[[Category: Wingfield PT]]
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[[Category: Wu, W]]
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[[Category: Wu W]]
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[[Category: Virus]]
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Current revision

HBV T=3 149C3A

6ui6, resolution 3.53Å

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