1mlu

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[[Image:1mlu.gif|left|200px]]
 
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==NITRIC OXIDE RECOMBINATION TO DOUBLE MUTANTS OF MYOGLOBIN: THE ROLE OF LIGAND DIFFUSION IN A FLUCTUATING HEME POCKET==
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The line below this paragraph, containing "STRUCTURE_1mlu", creates the "Structure Box" on the page.
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<StructureSection load='1mlu' size='340' side='right'caption='[[1mlu]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1mlu]] 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=1MLU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MLU FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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>
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<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>
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{{STRUCTURE_1mlu| PDB=1mlu | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mlu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mlu OCA], [https://pdbe.org/1mlu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mlu RCSB], [https://www.ebi.ac.uk/pdbsum/1mlu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mlu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ml/1mlu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1mlu ConSurf].
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<div style="clear:both"></div>
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'''NITRIC OXIDE RECOMBINATION TO DOUBLE MUTANTS OF MYOGLOBIN: THE ROLE OF LIGAND DIFFUSION IN A FLUCTUATING HEME POCKET'''
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==See Also==
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*[[Myoglobin 3D structures|Myoglobin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Picosecond recombination of nitric oxide to the double mutants of myoglobin, His64Gly-Val68Ala and His64Gly.Val68Ile, at E7 and E11, has been studied experimentally and by computation. It is shown that distal residues have a profound effect on NO recombination. Recombination in the mutants may be explained in terms of fluctuating free volume and structure of the heme pocket. The double mutants provide insight into the effects of free volume and steric hindrance on rates of ligand rebinding following photolysis. Water molecules of the first solvation shell replace surface residues deleted by mutation and can block apparent holes in the protein structure. Thus, water molecules extend the time required for ligands to escape significantly to a nanosecond time scale, which is much longer than would be expected for an open heme pocket. Both nearly exponential (G64A68) and markedly nonexponential (native and G64I68) kinetics are observed, a result at variance with expectation from the model of Petrich et al. [Petrich, J.W., Lambry, J.C., Kuczera, K., Karplus, M., Poyart, C., &amp; Martin, J.L. (1991) Biochemistry 30, 3975-3987], which attributes nonexponential kinetics to proximal effects.
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[[Category: Large Structures]]
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==About this Structure==
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1MLU is a [[Single protein]] 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=1MLU OCA].
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==Reference==
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Nitric oxide recombination to double mutants of myoglobin: role of ligand diffusion in a fluctuating heme pocket., Carlson ML, Regan R, Elber R, Li H, Phillips GN Jr, Olson JS, Gibson QH, Biochemistry. 1994 Sep 6;33(35):10597-606. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8075059 8075059]
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[[Category: Physeter catodon]]
[[Category: Physeter catodon]]
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[[Category: Single protein]]
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[[Category: Phillips Jr GN]]
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[[Category: Jr., G N.Phillips.]]
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[[Category: Quillin ML]]
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[[Category: Quillin, M L.]]
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[[Category: Oxygen storage]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:23:50 2008''
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NITRIC OXIDE RECOMBINATION TO DOUBLE MUTANTS OF MYOGLOBIN: THE ROLE OF LIGAND DIFFUSION IN A FLUCTUATING HEME POCKET

PDB ID 1mlu

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