1d1a

<StructureSection load='1d1a' size='340' side='right' caption='[[1d1a]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[1d1a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D1A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1D1A FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAE:O,P-DINITROPHENYL+AMINOETHYLDIPHOSPHATE-BERYLLIUM+TRIFLUORIDE'>DAE</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">[[1mmd|1mmd]], [[1mmn|1mmn]], [[1d0x|1d0x]], [[1d0y|1d0y]], [[1d0z|1d0z]], [[1d1b|1d1b]], [[1d1c|1d1c]]</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=1d1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d1a OCA], [http://pdbe.org/1d1a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1d1a RCSB], [http://www.ebi.ac.uk/pdbsum/1d1a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1d1a ProSAT]</span></td></tr>

[[http://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.

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== Publication Abstract from PubMed ==

The 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).

 

== References ==

[[Category: Atcc 11735]]

[[Category: Bauer, C B]]

[[Category: Gulick, A M]]

[[Category: Pate, E]]

[[Category: Rayment, I]]

[[Category: Thoden, J B]]

[[Category: Yount, R G]]

[[Category: Nanolog]]