1o1a: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1o1a.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1o1a", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_1o1a|  PDB=1o1a  |  SCENE=  }}
-'''MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE'''
+==MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE==
+<SX load='1o1a' size='340' side='right' viewer='molstar' caption='[[1o1a]], [[Resolution|resolution]] 70.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1o1a]] is a 32 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O1A FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 70&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></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=1o1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o1a OCA], [https://pdbe.org/1o1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o1a RCSB], [https://www.ebi.ac.uk/pdbsum/1o1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o1a ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://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.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o1/1o1a_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1o1a ConSurf].
+<div style="clear:both"></div>
+<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.
-==Overview==
+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>
-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.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-O1A is a [[Protein complex]] structure of sequences 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=1O1A OCA].
+</div>
+<div class="pdbe-citations 1o1a" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/12160705 12160705]
+*[[Actin 3D structures|Actin 3D structures]]
+*[[Myosin 3D Structures|Myosin 3D Structures]]
+== References ==
+<references/>
+__TOC__
+</SX>
 [[Category: Gallus gallus]]
+[[Category: Large Structures]]
 [[Category: Oryctolagus cuniculus]]
-[[Category: Protein complex]]
+[[Category: Chen LF]]
-[[Category: Chen, L F.]]
+[[Category: Reedy MC]]
-[[Category: Reedy, M C.]]
+[[Category: Reedy MK]]
-[[Category: Reedy, M K.]]
+[[Category: Taylor KA]]
-[[Category: Taylor, K A.]]
+[[Category: Winkler H]]
-[[Category: Winkler, H.]]
-[[Category: Actin-myosin complex in situ in muscle]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:13:59 2008''