1mgn: Difference between revisions

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 ==HIS64(E7)-> TYR APOMYOGLOBIN AS A REAGENT FOR MEASURING RATES OF HEMIN DISSOCIATION==
-<StructureSection load='1mgn' size='340' side='right' caption='[[1mgn]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='1mgn' size='340' side='right'caption='[[1mgn]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mgn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phycd Phycd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MGN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MGN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mgn]] 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=1MGN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MGN FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</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='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=1mgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mgn OCA], [http://pdbe.org/1mgn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mgn RCSB], [http://www.ebi.ac.uk/pdbsum/1mgn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mgn ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1mgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mgn OCA], [https://pdbe.org/1mgn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mgn RCSB], [https://www.ebi.ac.uk/pdbsum/1mgn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mgn ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
+[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]]
@@ Line 19: / Line 20: @@
 </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=1mgn ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-To develop an assay for hemin dissociation, His64(E7) was replaced by Tyr in sperm whale myoglobin producing a holoprotein with a distinct green color due to an intense absorption band at 600 nm. Val68(E11) was replaced by Phe in the same protein to increase its stability. When excess Tyr64-Val68 apoglobin is mixed with either metmyoglobin or methemoglobin, the solution turns from brown to green, and the absorbance changes can be used to measure complete time courses for hemin dissociation from either holoprotein. This assay has been used to measure rates of hemin dissociation from native metmyoglobin, four myoglobin mutants (Ala64(E7), Ala68(E11), Phe68(E11), and Glu45(CD3)), native methemoglobin, valence hybrid hemoglobins, and two mutant hemoglobins ((alpha(Gly-E7)beta(native))2, and (alpha(native)beta(Gly-E7))2). Two kinetic phases were observed for hemin dissociation from native human hemoglobin at pH 7.0 and 37 degrees C. Valence and mutant hybrid hemoglobins were used to assign the faster phase (k = 7.8 +/- 2.0 h-1) to hemin dissociation from ferric beta subunits and the slower (k = 0.6 +/- 0.15 h-1) to dissociation from alpha subunits. The corresponding rate for wild-type metmyoglobin is 0.007 +/- 0.004 h-1.
-His64(E7)--&gt;Tyr apomyoglobin as a reagent for measuring rates of hemin dissociation.,Hargrove MS, Singleton EW, Quillin ML, Ortiz LA, Phillips GN Jr, Olson JS, Mathews AJ J Biol Chem. 1994 Feb 11;269(6):4207-14. PMID:8307983<ref>PMID:8307983</ref>
+==See Also==
+*[[Myoglobin 3D structures|Myoglobin 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1mgn" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Phycd]]
+[[Category: Large Structures]]
-[[Category: Hargrove, M S]]
+[[Category: Physeter catodon]]
-[[Category: Phillips, G N]]
+[[Category: Hargrove MS]]
-[[Category: Quillin, M L]]
+[[Category: Phillips Jr GN]]
-[[Category: Oxygen transport]]
+[[Category: Quillin ML]]