2g0s: Difference between revisions

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-{{Seed}}
-[[Image:2g0s.png|left|200px]]
-<!--
+==Unphotolyzed CO-bound L29F Myoglobin, crystal 2==
-The line below this paragraph, containing "STRUCTURE_2g0s", creates the "Structure Box" on the page.
+<StructureSection load='2g0s' size='340' side='right'caption='[[2g0s]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2g0s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G0S FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-{{STRUCTURE_2g0s|  PDB=2g0s  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2g0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g0s OCA], [https://pdbe.org/2g0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g0s RCSB], [https://www.ebi.ac.uk/pdbsum/2g0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g0s ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
+== 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/g0/2g0s_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=2g0s ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Picosecond time-resolved crystallography was used to follow the dissociation of carbon monoxide from the heme pocket of a mutant sperm whale myoglobin and the resultant conformational changes. Electron-density maps have previously been created at various time points and used to describe amino-acid side-chain and carbon monoxide movements. In this work, difference refinement was employed to generate atomic coordinates at each time point in order to create a more explicit quantitative representation of the photo-dissociation process. After photolysis the carbon monoxide moves to a docking site, causing rearrangements in the heme-pocket residues, the coordinate changes of which can be plotted as a function of time. These include rotations of the heme-pocket phenylalanine concomitant with movement of the distal histidine toward the solvent, potentially allowing carbon monoxide movement in and out of the protein and proximal displacement of the heme iron. The degree of relaxation toward the intermediate and deoxy states was probed by analysis of the coordinate movements in the time-resolved models, revealing a non-linear progression toward the unbound state with coordinate movements that begin in the heme-pocket area and then propagate throughout the rest of the protein.
-===Unphotolyzed CO-bound L29F Myoglobin, crystal 2===
+Time-dependent atomic coordinates for the dissociation of carbon monoxide from myoglobin.,Aranda R 4th, Levin EJ, Schotte F, Anfinrud PA, Phillips GN Jr Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):776-83. Epub 2006, Jun 20. PMID:16790933<ref>PMID:16790933</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2g0s" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_16790933}}, adds the Publication Abstract to the page
+*[[Myoglobin 3D structures|Myoglobin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 16790933 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16790933}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-G0S is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G0S OCA].
-==Reference==
-<ref group="xtra">PMID:16790933</ref><references group="xtra"/>
 [[Category: Physeter catodon]]
-[[Category: Anfinrud, P A.]]
+[[Category: Anfinrud PA]]
-[[Category: Aranda, R.]]
+[[Category: Aranda R]]
-[[Category: Levin, E J.]]
+[[Category: Levin EJ]]
-[[Category: Phillips, G N.]]
+[[Category: Phillips Jr GN]]
-[[Category: Schotte, F.]]
+[[Category: Schotte F]]
-[[Category: Difference refinement]]
-[[Category: Intermediate state]]
-[[Category: Myoglobin]]
-[[Category: Structure-function relationship]]
-[[Category: Time-resolved crystallography]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:57:52 2009''