7kog

<table><tr><td colspan='2'>[[7kog]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lethocerus_indicus Lethocerus indicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KOG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KOG FirstGlance]. <br>

</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=7kog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kog OCA], [https://pdbe.org/7kog PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kog RCSB], [https://www.ebi.ac.uk/pdbsum/7kog PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kog ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The atomic structure of the complete myosin tail within thick filaments isolated from Lethocerus indicus flight muscle is described and compared to crystal structures of recombinant, human cardiac myosin tail segments. Overall, the agreement is good with three exceptions: the proximal S2, in which the filament has heads attached but the crystal structure doesn't, and skip regions 2 and 4. At the head-tail junction, the tail alpha-helices are asymmetrically structured encompassing well-defined unfolding of 12 residues for one myosin tail, approximately 4 residues of the other, and different degrees of alpha-helix unwinding for both tail alpha-helices, thereby providing an atomic resolution description of coiled-coil "uncoiling" at the head-tail junction. Asymmetry is observed in the nonhelical C termini; one C-terminal segment is intercalated between ribbons of myosin tails, the other apparently terminating at Skip 4 of another myosin tail. Between skip residues, crystal and filament structures agree well. Skips 1 and 3 also agree well and show the expected alpha-helix unwinding and coiled-coil untwisting in response to skip residue insertion. Skips 2 and 4 are different. Skip 2 is accommodated in an unusual manner through an increase in alpha-helix radius and corresponding reduction in rise/residue. Skip 4 remains helical in one chain, with the other chain unfolded, apparently influenced by the acidic myosin C terminus. The atomic model may shed some light on thick filament mechanosensing and is a step in understanding the complex roles that thick filaments of all species undergo during muscle contraction.

 

== References ==

[[Category: Daneshparvar, N]]

[[Category: Hu, Z]]

[[Category: Rahmani, H]]

[[Category: Taylor, D]]

[[Category: Taylor, K A]]

[[Category: Striated muscle]]