1alm: Difference between revisions
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{{Theoretical_model}} | |||
==THE STRUCTURE OF THE ACTO-MYOSIN SUBFRAGMENT-ONE COMPLEX. RESULTS OF SEARCHES USING DATA FROM ELECTRON MICROSCOPY AND X-RAY CRYSTALLOGRAPHY. THEORETICAL MODEL, ALPHA CARBONS.== | ==THE STRUCTURE OF THE ACTO-MYOSIN SUBFRAGMENT-ONE COMPLEX. RESULTS OF SEARCHES USING DATA FROM ELECTRON MICROSCOPY AND X-RAY CRYSTALLOGRAPHY. THEORETICAL MODEL, ALPHA CARBONS.== | ||
<StructureSection load='1alm' size='340' side='right' caption='[[1alm]]' scene=''> | <StructureSection load='1alm' size='340' side='right'caption='[[1alm]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>The July 2001 RCSB PDB [ | <table><tr><td colspan='2'>The July 2001 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Actin'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2001_7 10.2210/rcsb_pdb/mom_2001_7]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ALM FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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=1alm FirstGlance], [https://www.ebi.ac.uk/pdbsum/1alm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1alm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1alm" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Theoretical Model]] | |||
[[Category: Actin]] | [[Category: Actin]] | ||
[[Category: Large Structures]] | |||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
[[Category: Mendelson, R A]] | |||
[[Category: Morris, E P]] | |||
Latest revision as of 12:46, 26 May 2021
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THE STRUCTURE OF THE ACTO-MYOSIN SUBFRAGMENT-ONE COMPLEX. RESULTS OF SEARCHES USING DATA FROM ELECTRON MICROSCOPY AND X-RAY CRYSTALLOGRAPHY. THEORETICAL MODEL, ALPHA CARBONS.THE STRUCTURE OF THE ACTO-MYOSIN SUBFRAGMENT-ONE COMPLEX. RESULTS OF SEARCHES USING DATA FROM ELECTRON MICROSCOPY AND X-RAY CRYSTALLOGRAPHY. THEORETICAL MODEL, ALPHA CARBONS.
Structural highlights
Publication Abstract from PubMedSurmises of how myosin subfragment 1 (S1) interacts with actin filaments in muscle contraction rest upon knowing the relative arrangement of the two proteins. Although there exist crystallographic structures for both S1 and actin, as well as electron microscopy data for the acto-S1 complex (AS1), modeling of this arrangement has so far only been done "by eye." Here we report fitted AS1 structures obtained using a quantitative method that is both more objective and makes more complete use of the data. Using undistorted crystallographic results, the best-fit AS1 structure shows significant differences from that obtained by visual fitting. The best fit is produced using the F-actin model of Holmes et al. [Holmes, K. C., Popp, D., Gebhard, W. & Kabsch, W. (1990) Nature (London) 347, 44-49]. S1 residues at the AS1 interface are now found at a higher radius as well as being translated axially and rotated azimuthally. Fits using S1 plus loops missing from the crystal structure were achieved using a homology search method to predict loop structures. These improved fits favor an arrangement in which the loop at the 50- to 20-kDa domain junction of S1 is located near the N terminus of actin. Rigid-body movements of the lower 50-kDa domain, which further improve the fit, produce closure of the large 50-kDa domain cleft and bring conserved residues in the lower 50-kDa domain into an apparently appropriate orientation for close interaction with actin. This finding supports the idea that binding of ATP to AS1 at the end of the ATPase cycle disrupts the actin binding site by changing the conformation of the 50-kDa cleft of S1. The structure of the acto-myosin subfragment 1 complex: results of searches using data from electron microscopy and x-ray crystallography.,Mendelson R, Morris EP Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8533-8. PMID:9238011[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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