1mvw

<StructureSection load='1mvw' size='340' side='right' caption='[[1mvw]], [[Resolution|resolution]] 70.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[1mvw]] is a 32 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MVW FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1m8q|1m8q]]</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=1mvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mvw OCA], [http://pdbe.org/1mvw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mvw RCSB], [http://www.ebi.ac.uk/pdbsum/1mvw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mvw ProSAT]</span></td></tr>

{{Large structure}}

[[http://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [[http://www.uniprot.org/uniprot/MYSS_CHICK MYSS_CHICK]] Muscle contraction. Myosin is a protein that binds to F-actin and has ATPase activity that is activated by F-actin.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Electron tomography, correspondence analysis, molecular model building, and real-space refinement provide detailed 3-D structures for in situ myosin crossbridges in the nucleotide-free state (rigor), thought to represent the end of the power stroke. Unaveraged tomograms from a 25-nm longitudinal section of insect flight muscle preserved native structural variation. Recurring crossbridge motifs that repeat every 38.7 nm along the actin filament were extracted from the tomogram and classified by correspondence analysis into 25 class averages, which improved the signal to noise ratio. Models based on the atomic structures of actin and of myosin subfragment 1 were rebuilt to fit 11 class averages. A real-space refinement procedure was applied to quantitatively fit the reconstructions and to minimize steric clashes between domains introduced during the fitting. These combined procedures show that no single myosin head structure can fit all the in situ crossbridges. The validity of the approach is supported by agreement of these atomic models with fluorescent probe data from vertebrate muscle as well as with data from regulatory light chain crosslinking between heads of smooth muscle heavy meromyosin when bound to actin.

Molecular modeling of averaged rigor crossbridges from tomograms of insect flight muscle.,Chen LF, Winkler H, Reedy MK, Reedy MC, Taylor KA J Struct Biol. 2002 Apr-May;138(1-2):92-104. PMID:12160705<ref>PMID:12160705</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1mvw" style="background-color:#fffaf0;"></div>

*[[Actin|Actin]]

*[[Myosin|Myosin]]

</StructureSection>

[[Category: Chen, L F]]

[[Category: Reedy, M C]]

[[Category: Reedy, M K]]

[[Category: Taylor, K A]]

[[Category: Winkler, H]]

[[Category: Contractile protein]]