1bmv
From Proteopedia
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| - | [[Image:1bmv.gif|left|200px]]<br /><applet load="1bmv" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1bmv, resolution 3.000Å" /> | ||
| - | '''PROTEIN-RNA INTERACTIONS IN AN ICOSAHEDRAL VIRUS AT 3.0 ANGSTROMS RESOLUTION'''<br /> | ||
| - | == | + | ==PROTEIN-RNA INTERACTIONS IN AN ICOSAHEDRAL VIRUS AT 3.0 ANGSTROMS RESOLUTION== |
| + | <StructureSection load='1bmv' size='340' side='right'caption='[[1bmv]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1bmv]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bean_pod_mottle_virus Bean pod mottle virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BMV FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[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=1bmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bmv OCA], [https://pdbe.org/1bmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bmv RCSB], [https://www.ebi.ac.uk/pdbsum/1bmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bmv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/POL2_BPMV POL2_BPMV] Movement protein: transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Acts by forming a tubular structure at the host plasmodesmata, enlarging it enough to allow free passage of virion capsids (By similarity). | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bm/1bmv_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bmv ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Nearly 20 percent of the packaged RNA in bean-pod mottle virus (BPMV) binds to the capsid interior in a symmetric fashion and is clearly visible in the electron density map. The RNA displaying icosahedral symmetry is single-stranded with well-defined polarity and stereochemical properties. Interactions with protein are dominated by nonbonding forces with few specific contacts. The tertiary and quaternary structures of the BPMV capsid proteins are similar to those observed in animal picornaviruses, supporting the close relation between plant comoviruses and animal picornaviruses established by previous biological studies. | Nearly 20 percent of the packaged RNA in bean-pod mottle virus (BPMV) binds to the capsid interior in a symmetric fashion and is clearly visible in the electron density map. The RNA displaying icosahedral symmetry is single-stranded with well-defined polarity and stereochemical properties. Interactions with protein are dominated by nonbonding forces with few specific contacts. The tertiary and quaternary structures of the BPMV capsid proteins are similar to those observed in animal picornaviruses, supporting the close relation between plant comoviruses and animal picornaviruses established by previous biological studies. | ||
| - | + | Protein-RNA interactions in an icosahedral virus at 3.0 A resolution.,Chen ZG, Stauffacher C, Li Y, Schmidt T, Bomu W, Kamer G, Shanks M, Lomonossoff G, Johnson JE Science. 1989 Jul 14;245(4914):154-9. PMID:2749253<ref>PMID:2749253</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1bmv" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bean pod mottle virus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bomu W]] | ||
| + | [[Category: Chen Z]] | ||
| + | [[Category: Johnson JE]] | ||
| + | [[Category: Kamer G]] | ||
| + | [[Category: Li Y]] | ||
| + | [[Category: Lomonossoff G]] | ||
| + | [[Category: Schmidt T]] | ||
| + | [[Category: Shanks M]] | ||
| + | [[Category: Stauffacher C]] | ||
Current revision
PROTEIN-RNA INTERACTIONS IN AN ICOSAHEDRAL VIRUS AT 3.0 ANGSTROMS RESOLUTION
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Categories: Bean pod mottle virus | Large Structures | Bomu W | Chen Z | Johnson JE | Kamer G | Li Y | Lomonossoff G | Schmidt T | Shanks M | Stauffacher C
