1mst: Difference between revisions
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<StructureSection load='1mst' size='340' side='right'caption='[[1mst]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='1mst' size='340' side='right'caption='[[1mst]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1mst]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1mst]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteriophage_ms2 Bacteriophage ms2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MST OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MST FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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=1mst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mst OCA], [https://pdbe.org/1mst PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mst RCSB], [https://www.ebi.ac.uk/pdbsum/1mst PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mst ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/COAT_BPMS2 COAT_BPMS2]] Forms the phage shell; binds to the phage RNA. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 12:29, 5 May 2021
CRYSTAL STRUCTURE OF MS2 CAPSIDS WITH MUTATIONS IN THE SUBUNIT FG LOOPCRYSTAL STRUCTURE OF MS2 CAPSIDS WITH MUTATIONS IN THE SUBUNIT FG LOOP
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 PubMedThe loop between the F and G beta strands (FG loop) of the bacteriophage MS2 coat protein subunit forms inter-subunit contacts around the 5-fold and 3-fold (quasi 6-fold) axes of the T=3 protein shell. In capsids, the loop is found in two very different conformations, one in B subunits, which form the 5-fold contact, and one in A and C subunits, which form the quasi 6-fold contact. One proline residue, Pro78, is strictly conserved in the coat protein of all related bacteriophages, and in the case of MS2 this proline residue is preceded by a cis peptide bond in the B subunit. In order to probe the role of the FG loop in capsid assembly, we have determined the crystal structures of two MS2 capsids, formed by coat proteins with mutations at two positions in the FG loop, P78N or E76D. These mutants show conformational changes in the FG loops that explain the reduced temperature stability of the capsids. The P78N mutant has a normal trans peptide bond at position 78. Crystal structures of MS2 capsids with mutations in the subunit FG loop.,Stonehouse NJ, Valegard K, Golmohammadi R, van den Worm S, Walton C, Stockley PG, Liljas L J Mol Biol. 1996 Feb 23;256(2):330-9. PMID:8594200[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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