1aq4: Difference between revisions

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 <StructureSection load='1aq4' size='340' side='right'caption='[[1aq4]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1aq4]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AQ4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1aq4]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_MS2 Escherichia phage MS2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AQ4 FirstGlance]. <br>
-</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=1aq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aq4 OCA], [https://pdbe.org/1aq4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aq4 RCSB], [https://www.ebi.ac.uk/pdbsum/1aq4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aq4 ProSAT]</span></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aq4 OCA], [https://pdbe.org/1aq4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aq4 RCSB], [https://www.ebi.ac.uk/pdbsum/1aq4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aq4 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/COAT_BPMS2 COAT_BPMS2]] Forms the phage shell; binds to the phage RNA.
+[https://www.uniprot.org/uniprot/CAPSD_BPMS2 CAPSD_BPMS2] Self-assembles to form the T=3 icosahedral virus shell that protects the viral nucleic acid. Acts as a translational repressor by binding with high specificity to a single stem-loop structure in the genomic RNA that contains the initiation codon of the gene for the viral replicase. Involved in virus assembly through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome.<ref>PMID:16531233</ref> <ref>PMID:18662904</ref> <ref>PMID:26608810</ref> <ref>PMID:8254664</ref> <ref>PMID:9245600</ref> <ref>PMID:9469847</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 18: / Line 19: @@
 </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=1aq4 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-In MS2 assembly of phage particles results from an interaction between a coat protein dimer and a stem-loop of the RNA genome (the operator hairpin). Amino acid residues Thr45, which is universally conserved among the small RNA phages, and Thr59 are part of the specific RNA binding pocket and interact directly with the RNA; the former through a hydrogen bond, the latter through hydrophobic contacts. The crystal structures of MS2 protein capsids formed by mutants Thr45Ala and Thr59Ser, both with and without the 19 nt wild-type operator hairpin bound, are reported here. The RNA hairpin binds to these mutants in a similar way to its binding to wild-type protein. In a companion paper both mutants are shown to be deficient in RNA binding in an in vivo assay, but in vitro the equilibrium dissociation constant is significantly higher than wild-type for the Thr45Ala mutant. The change in binding affinity of the Thr45Ala mutant is probably a direct consequence of removal of direct hydrogen bonds between the protein and the RNA. The properties of the Thr59Ser mutant are more difficult to explain, but are consistent with a loss of non-polar contact.
-Crystal structures of MS2 coat protein mutants in complex with wild-type RNA operator fragments.,van den Worm SH, Stonehouse NJ, Valegard K, Murray JB, Walton C, Fridborg K, Stockley PG, Liljas L Nucleic Acids Res. 1998 Mar 1;26(5):1345-51. PMID:9469847<ref>PMID:9469847</ref>
+==See Also==
+*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1aq4" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Escherichia phage MS2]]
 [[Category: Large Structures]]
-[[Category: Liljas, L]]
+[[Category: Liljas L]]
-[[Category: Stonehouse, N J]]
+[[Category: Stonehouse NJ]]
-[[Category: Valegard, K]]
+[[Category: Valegard K]]
-[[Category: Worm, S H.Van Den]]
+[[Category: Van Den Worm SH]]
-[[Category: Coat protein]]
-[[Category: Icosahedral virus]]
-[[Category: Rna fragment]]
-[[Category: Rna-binding]]
-[[Category: Viral protein capsid]]
-[[Category: Virus-rna complex]]