2y9e: Difference between revisions
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<StructureSection load='2y9e' size='340' side='right'caption='[[2y9e]], [[Resolution|resolution]] 3.40Å' scene=''> | <StructureSection load='2y9e' size='340' side='right'caption='[[2y9e]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2y9e]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2y9e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dicdi Dicdi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y9E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y9E FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mne|1mne]], [[1d1c|1d1c]], [[1w9l|1w9l]], [[1mmn|1mmn]], [[1vom|1vom]], [[2jhr|2jhr]], [[2aka|2aka]], [[2y8i|2y8i]], [[1w9j|1w9j]], [[2x9h|2x9h]], [[1fmv|1fmv]], [[1mma|1mma]], [[2xo8|2xo8]], [[2y0r|2y0r]], [[1mmg|1mmg]], [[1w9i|1w9i]], [[1w9k|1w9k]], [[1mnd|1mnd]], [[1jx2|1jx2]], [[1q5g|1q5g]], [[1d0y|1d0y]], [[2jj9|2jj9]], [[2xel|2xel]], [[1lvk|1lvk]], [[1jwy|1jwy]], [[1yv3|1yv3]], [[1fmw|1fmw]], [[1d0x|1d0x]], [[1d1b|1d1b]], [[1g8x|1g8x]], [[1d1a|1d1a]], [[1d0z|1d0z]], [[1mmd|1mmd]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mne|1mne]], [[1d1c|1d1c]], [[1w9l|1w9l]], [[1mmn|1mmn]], [[1vom|1vom]], [[2jhr|2jhr]], [[2aka|2aka]], [[2y8i|2y8i]], [[1w9j|1w9j]], [[2x9h|2x9h]], [[1fmv|1fmv]], [[1mma|1mma]], [[2xo8|2xo8]], [[2y0r|2y0r]], [[1mmg|1mmg]], [[1w9i|1w9i]], [[1w9k|1w9k]], [[1mnd|1mnd]], [[1jx2|1jx2]], [[1q5g|1q5g]], [[1d0y|1d0y]], [[2jj9|2jj9]], [[2xel|2xel]], [[1lvk|1lvk]], [[1jwy|1jwy]], [[1yv3|1yv3]], [[1fmw|1fmw]], [[1d0x|1d0x]], [[1d1b|1d1b]], [[1g8x|1g8x]], [[1d1a|1d1a]], [[1d0z|1d0z]], [[1mmd|1mmd]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Myosin_ATPase Myosin ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.1 3.6.4.1] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2y9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y9e OCA], [https://pdbe.org/2y9e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y9e RCSB], [https://www.ebi.ac.uk/pdbsum/2y9e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y9e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/MYS2_DICDI MYS2_DICDI]] Myosin is a protein that binds to actin and has ATPase activity that is activated by actin. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 21: | Line 21: | ||
==See Also== | ==See Also== | ||
*[[Myosin|Myosin]] | *[[Myosin 3D Structures|Myosin 3D Structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 18:02, 17 November 2021
Structural basis for the allosteric interference of myosin function by mutants G680A and G680V of Dictyostelium myosin-2Structural basis for the allosteric interference of myosin function by mutants G680A and G680V of Dictyostelium myosin-2
Structural highlights
Function[MYS2_DICDI] Myosin is a protein that binds to actin and has ATPase activity that is activated by actin. Publication Abstract from PubMedThe cold-sensitive single-residue mutation of glycine 680 in the reactive thiol region of Dictyostelium discoideum myosin-2 or the corresponding conserved glycine in other myosin isoforms has been reported to interfere with motor function. Here we present the x-ray structures of myosin motor domain mutants G680A in the absence and presence of nucleotide as well as the apo structure of mutant G680V. Our results show that the Gly-680 mutations lead to uncoupling of the reactive thiol region from the surrounding structural elements. Structural and functional data indicate that the mutations induce the preferential population of a state that resembles the ADP-bound state. Moreover, the Gly-680 mutants display greatly reduced dynamic properties, which appear to be related to the recovery of myosin motor function at elevated temperatures. Structural Basis for the Allosteric Interference of Myosin Function by Reactive Thiol Region Mutations G680A and G680V.,Preller M, Bauer S, Adamek N, Fujita-Becker S, Fedorov R, Geeves MA, Manstein DJ J Biol Chem. 2011 Oct 7;286(40):35051-60. Epub 2011 Aug 13. PMID:21841195[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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