1aq4: Difference between revisions
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<StructureSection load='1aq4' size='340' side='right' caption='[[1aq4]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='1aq4' size='340' side='right' caption='[[1aq4]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1aq4]] is a 5 chain structure | <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 [http://oca.weizmann.ac.il/oca-docs/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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aq4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aq4 RCSB], [http://www.ebi.ac.uk/pdbsum/1aq4 PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aq4 OCA], [http://pdbe.org/1aq4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aq4 RCSB], [http://www.ebi.ac.uk/pdbsum/1aq4 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1aq4" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Stonehouse, N]] | [[Category: Stonehouse, N]] | ||
[[Category: Valegard, K]] | [[Category: Valegard, K]] | ||
Revision as of 06:21, 10 September 2015
STRUCTURE OF A MS2 COAT PROTEIN MUTANT IN COMPLEX WITH AN RNA OPERATORSTRUCTURE OF A MS2 COAT PROTEIN MUTANT IN COMPLEX WITH AN RNA OPERATOR
Structural highlights
Function[COAT_BPMS2] Forms the phage shell; binds to the phage RNA. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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