1lvk: Difference between revisions

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<StructureSection load='1lvk' size='340' side='right'caption='[[1lvk]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1lvk' size='340' side='right'caption='[[1lvk]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1lvk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LVK FirstGlance]. <br>
<table><tr><td colspan='2'>[[1lvk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LVK FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MNT:2(3)-O-N-METHYLANTHRANILOYL-ADENOSINE-5-DIPHOSPHATE'>MNT</scene></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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MNT:2(3)-O-N-METHYLANTHRANILOYL-ADENOSINE-5-DIPHOSPHATE'>MNT</scene></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=1lvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lvk OCA], [https://pdbe.org/1lvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lvk RCSB], [https://www.ebi.ac.uk/pdbsum/1lvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lvk ProSAT]</span></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=1lvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lvk OCA], [https://pdbe.org/1lvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lvk RCSB], [https://www.ebi.ac.uk/pdbsum/1lvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lvk 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.  
[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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1lvk ConSurf].
</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=1lvk ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mant (2'(3')-O-(N-methylanthraniloyl)) labeled nucleotides have proven to be useful tools in the study of the kinetic mechanism of the myosin ATPase by fluorescence spectroscopy. The sensitivity of the mant fluorophore to its local environment also makes it suitable to investigate the exposure of bound nucleotides to solvent from collisional quenching measurements. Here we present the crystal structure of mant-ADP and beryllium fluoride complexed with Dictyostelium discoideum myosin motor domain (S1dC) at 1.9 A resolution. We complement the structural approach with an investigation of the accessibility of the mant moiety to solvent using acrylamide quenching of fluorescence emission. In contrast to rabbit skeletal myosin subfragment 1, where the mant group is protected from acrylamide (Ksv=0.2 M-1), the fluorophore is relatively exposed when bound to Dictyostelium myosin motor domain (Ksv= 1.4 M-1). Differences between the Dictyostelium structure and that of vertebrate skeletal subfragment 1, in the region of the nucleotide binding pocket, are proposed as an explanation for the differences observed in the solvent accessibility of complexed mant-nucleotides. We conclude that protection of the mant group from acrylamide quenching does not report on overall closure of the nucleotide binding pocket but reflects more local structural changes.
X-ray crystal structure and solution fluorescence characterization of Mg.2'(3')-O-(N-methylanthraniloyl) nucleotides bound to the Dictyostelium discoideum myosin motor domain.,Bauer CB, Kuhlman PA, Bagshaw CR, Rayment I J Mol Biol. 1997 Dec 5;274(3):394-407. PMID:9405148<ref>PMID:9405148</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1lvk" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Myosin 3D Structures|Myosin 3D Structures]]
*[[Myosin 3D Structures|Myosin 3D Structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 11735]]
[[Category: Dictyostelium discoideum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bagshaw, C R]]
[[Category: Bagshaw CR]]
[[Category: Bauer, C B]]
[[Category: Bauer CB]]
[[Category: Kuhlman, P A]]
[[Category: Kuhlman PA]]
[[Category: Rayment, I]]
[[Category: Rayment I]]
[[Category: Actin-binding]]
[[Category: Atpase]]
[[Category: Coiled coil]]
[[Category: Contractile protein]]
[[Category: Dictyostelium]]
[[Category: Mant]]
[[Category: Motor]]
[[Category: Myosin]]

Latest revision as of 10:36, 14 February 2024

X-RAY CRYSTAL STRUCTURE OF THE MG (DOT) 2'(3')-O-(N-METHYLANTHRANILOYL) NUCLEOTIDE BOUND TO DICTYOSTELIUM DISCOIDEUM MYOSIN MOTOR DOMAINX-RAY CRYSTAL STRUCTURE OF THE MG (DOT) 2'(3')-O-(N-METHYLANTHRANILOYL) NUCLEOTIDE BOUND TO DICTYOSTELIUM DISCOIDEUM MYOSIN MOTOR DOMAIN

Structural highlights

1lvk is a 1 chain structure with sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MYS2_DICDI Myosin is a protein that binds to actin and has ATPase activity that is activated by actin.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1lvk, resolution 1.90Å

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