1xok: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(One intermediate revision by the same user not shown)
Line 3: Line 3:
<StructureSection load='1xok' size='340' side='right'caption='[[1xok]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='1xok' size='340' side='right'caption='[[1xok]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1xok]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XOK FirstGlance]. <br>
<table><tr><td colspan='2'>[[1xok]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Alfalfa_mosaic_virus_(strain_YSMV) Alfalfa mosaic virus (strain YSMV)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XOK FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></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]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</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=1xok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xok OCA], [https://pdbe.org/1xok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xok RCSB], [https://www.ebi.ac.uk/pdbsum/1xok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xok 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=1xok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xok OCA], [https://pdbe.org/1xok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xok RCSB], [https://www.ebi.ac.uk/pdbsum/1xok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xok ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CAPSD_AMVYS CAPSD_AMVYS]] Capsid protein. Binds to the to the 3' end of the nonpolyadenylated viral RNA and is involved in viral RNA translation initiation. Probably binds RNA and plays a role in packaging (By similarity).  
[https://www.uniprot.org/uniprot/CAPSD_AMVYS CAPSD_AMVYS] Capsid protein. Binds to the to the 3' end of the nonpolyadenylated viral RNA and is involved in viral RNA translation initiation. Probably binds RNA and plays a role in packaging (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Alfalfa mosaic virus genomic RNAs are infectious only when the viral coat protein binds to the RNA 3' termini. The crystal structure of an alfalfa mosaic virus RNA-peptide complex reveals that conserved AUGC repeats and Pro-Thr-x-Arg-Ser-x-x-Tyr coat protein amino acids cofold upon interacting. Alternating AUGC residues have opposite orientation, and they base pair in different adjacent duplexes. Localized RNA backbone reversals stabilized by arginine-guanine interactions place the adenosines and guanines in reverse order in the duplex. The results suggest that a uniform, organized 3' conformation, similar to that found on viral RNAs with transfer RNA-like ends, may be essential for replication.
 
Cofolding organizes alfalfa mosaic virus RNA and coat protein for replication.,Guogas LM, Filman DJ, Hogle JM, Gehrke L Science. 2004 Dec 17;306(5704):2108-11. PMID:15604410<ref>PMID:15604410</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1xok" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Filman, D J]]
[[Category: Filman DJ]]
[[Category: Gehrke, L]]
[[Category: Gehrke L]]
[[Category: Guogas, L M]]
[[Category: Guogas LM]]
[[Category: Hogle, J M]]
[[Category: Hogle JM]]
[[Category: Alpha helix]]
[[Category: Atypical rna duplex]]
[[Category: Protein-rna complex]]
[[Category: Viral protein-rna complex]]

Latest revision as of 11:52, 14 February 2024

crystal structure of alfalfa mosaic virus RNA 3'UTR in complex with coat protein N terminal peptidecrystal structure of alfalfa mosaic virus RNA 3'UTR in complex with coat protein N terminal peptide

Structural highlights

1xok is a 4 chain structure with sequence from Alfalfa mosaic virus (strain YSMV). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CAPSD_AMVYS Capsid protein. Binds to the to the 3' end of the nonpolyadenylated viral RNA and is involved in viral RNA translation initiation. Probably binds RNA and plays a role in packaging (By similarity).

1xok, resolution 3.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA