1d1b: Difference between revisions
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<StructureSection load='1d1b' size='340' side='right'caption='[[1d1b]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1d1b' size='340' side='right'caption='[[1d1b]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1d1b]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1d1b]] 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=1D1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D1B FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAQ:O,P-DINITROPHENYL+AMINOPROPYLDIPHOSPHATE+BERYLLIUM+TRIFLUORIDE'>DAQ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAQ:O,P-DINITROPHENYL+AMINOPROPYLDIPHOSPHATE+BERYLLIUM+TRIFLUORIDE'>DAQ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d0x|1d0x]], [[1d0y|1d0y]], [[1d0z|1d0z]], [[1d1a|1d1a]], [[1d1c|1d1c]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1d0x|1d0x]], [[1d0y|1d0y]], [[1d0z|1d0z]], [[1d1a|1d1a]], [[1d1c|1d1c]]</div></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=1d1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d1b OCA], [https://pdbe.org/1d1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d1b RCSB], [https://www.ebi.ac.uk/pdbsum/1d1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d1b 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. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 12:15, 8 September 2021
DICTYOSTELIUM MYOSIN S1DC (MOTOR DOMAIN FRAGMENT) COMPLEXED WITH O,P-DINITROPHENYL AMINOPROPYLDIPHOSPHATE BERYLLIUM TRIFLUORIDE.DICTYOSTELIUM MYOSIN S1DC (MOTOR DOMAIN FRAGMENT) COMPLEXED WITH O,P-DINITROPHENYL AMINOPROPYLDIPHOSPHATE BERYLLIUM TRIFLUORIDE.
Structural highlights
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. Publication Abstract from PubMedThe three-dimensional structures of the truncated myosin head from Dictyostelium discoideum myosin II complexed with dinitrophenylaminoethyl-, dinitrophenylaminopropyl-, o-nitrophenylaminoethyl-, m-nitrophenylaminoethyl-, p-nitrophenylaminoethyl-, and o-nitrophenyl-N-methyl-aminoethyl-diphosphate.beryllium fluoride have been determined to better than 2.3-A resolution. The structure of the protein and nucleotide binding pocket in these complexes is very similar to that of S1dC.ADP.BeF(x) (Fisher, A. J., Smith, C. A., Thoden, J., Smith, R., Sutoh, K., Holden, H. M., and Rayment, I. (1995) Biochemistry 34, 8960-8972). The position of the triphosphate-like moiety is essentially identical in all complexes. Furthermore, the alkyl-amino group plays the same role as the ribose by linking the triphosphate to the adenine binding pocket; however, none of the phenyl groups lie in the same position as adenine in S1dC.MgADP.BeF(x), even though several of these nucleotide analogs are functionally equivalent to ATP. Rather the former location of adenine is occupied by water in the nanolog complexes, and the phenyl groups are organized in a manner that attempts to optimize their hydrogen bonding interactions with this constellation of solvent molecules. A comparison of the kinetic and structural properties of the nanologs relative to ATP suggests that the ability of a substrate to sustain tension and to generate movement correlates with a well defined interaction with the active site water structure observed in S1dC.MgADP.BeF(x). X-ray structures of the Dictyostelium discoideum myosin motor domain with six non-nucleotide analogs.,Gulick AM, Bauer CB, Thoden JB, Pate E, Yount RG, Rayment I J Biol Chem. 2000 Jan 7;275(1):398-408. PMID:10617631[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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