1myj: Difference between revisions

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-[[Image:1myj.gif|left|200px]]
-<!--
+==DISTAL POLARITY IN LIGAND BINDING TO MYOGLOBIN: STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF A THREONINE68(E11) MUTANT==
-The line below this paragraph, containing "STRUCTURE_1myj", creates the "Structure Box" on the page.
+<StructureSection load='1myj' size='340' side='right'caption='[[1myj]], [[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'>[[1myj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MYJ 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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-{{STRUCTURE_1myj|  PDB=1myj  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1myj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1myj OCA], [https://pdbe.org/1myj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1myj RCSB], [https://www.ebi.ac.uk/pdbsum/1myj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1myj ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MYG_PIG MYG_PIG] 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/my/1myj_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=1myj ConSurf].
+<div style="clear:both"></div>
-'''DISTAL POLARITY IN LIGAND BINDING TO MYOGLOBIN: STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF A THREONINE68(E11) MUTANT'''
+==See Also==
+*[[Myoglobin 3D structures|Myoglobin 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-Site-directed mutagenesis studies have confirmed that the distal histidine in myoglobin stabilizes bound O2 by hydrogen bonding and have suggested that it is the polar character of the imidazole side chain rather than its size that limits the rate of ligand entry into the protein. We constructed an isosteric Val68 to Thr replacement in pig myoglobin (i) to investigate whether the O2 affinity could be increased by the introduction of a second hydrogen-bonding group into the distal heme pocket and (ii) to examine the influence of polarity on the ligand binding rates more rigorously. The 1.9-A crystal structure of Thr68 aquometmyoglobin confirms that the mutant and wild-type proteins are essentially isostructural and reveals that the beta-OH group of Thr68 is in a position to form hydrogen-bonding interactions both with the coordinated water molecule and with the main chain greater than C=O of residue 64. The rate of azide binding to the ferric form of the Thr68 mutant was 60-fold lower than that for the wild-type protein, consistent with the proposed stabilization of the coordinated water molecule. However, bound O2 is destabilized in the ferrous form of the mutant protein. The observed 17-fold lowering of the O2 affinity may be a consequence of the hydrogen-bonding interaction made between the Thr68 beta-OH group and the carbonyl oxygen of residue 64. Overall association rate constants for O2, NO, and alkyl isocyanide binding to ferrous pig myoglobin were 3-10-fold lower for the mutant compared to the wild-type protein, whereas that for CO binding was little affected.(ABSTRACT TRUNCATED AT 250 WORDS)
+[[Category: Large Structures]]
-==About this Structure==
-MYJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MYJ OCA].
-==Reference==
-Distal pocket polarity in ligand binding to myoglobin: structural and functional characterization of a threonine68(E11) mutant., Smerdon SJ, Dodson GG, Wilkinson AJ, Gibson QH, Blackmore RS, Biochemistry. 1991 Jun 25;30(25):6252-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1905570 1905570]
-[[Category: Single protein]]
 [[Category: Sus scrofa]]
-[[Category: Dauter, Z.]]
+[[Category: Dauter Z]]
-[[Category: Oldfield, T J.]]
+[[Category: Oldfield TJ]]
-[[Category: Petratos, K.]]
+[[Category: Petratos K]]
-[[Category: Smerdon, S J.]]
+[[Category: Smerdon SJ]]
-[[Category: Wilkinson, A J.]]
+[[Category: Wilkinson AJ]]
-[[Category: Wilson, K S.]]
+[[Category: Wilson KS]]
-[[Category: Oxygen storage]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:52:14 2008''