2blh

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[[Image:2blh.jpg|left|200px]]
 
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{{Structure
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==Ligand Migration and Protein Fluctuations in Myoglobin Mutant L29W==
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|PDB= 2blh |SIZE=350|CAPTION= <scene name='initialview01'>2blh</scene>, resolution 1.77&Aring;
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<StructureSection load='2blh' size='340' side='right'caption='[[2blh]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Hem+Binding+Site+For+Chain+A'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>
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<table><tr><td colspan='2'>[[2blh]] 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=2BLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BLH FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.77&#8491;</td></tr>
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|GENE=
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<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></td></tr>
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|DOMAIN=
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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=2blh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2blh OCA], [https://pdbe.org/2blh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2blh RCSB], [https://www.ebi.ac.uk/pdbsum/2blh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2blh ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2blh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2blh OCA], [http://www.ebi.ac.uk/pdbsum/2blh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2blh RCSB]</span>
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== Function ==
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}}
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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/bl/2blh_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=2blh ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We have determined eight X-ray structures of myoglobin mutant L29W at various experimental conditions. In addition, infrared spectroscopic experiments are presented, which are discussed in the light of the X-ray structures. Two distinct conformations of the CO-ligated protein were identified, giving rise to two stretching bands of heme-bound CO. If L29W MbCO crystals are illuminated around 180 K, a deoxy species is formed. The CO molecules migrate to the proximal side of the heme and remain trapped in the so-called Xe1 cavity upon temperature decrease to 105 K. The structure of this photoproduct is almost identical to the equilibrium high-temperature deoxy Mb structure. If the temperature is cycled to increasingly higher values, CO recombination is observed. Three intermediate structures have been determined during the rebinding process. Efficient recombination occurs only above 180 K, the characteristic temperature for the onset of protein dynamics. Rebinding is remarkably slow because bulky residues His64 and Trp29 block important migration pathways of the CO molecule.
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'''LIGAND MIGRATION AND PROTEIN FLUCTUATIONS IN MYOGLOBIN MUTANT L29W'''
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Ligand migration and protein fluctuations in myoglobin mutant L29W.,Nienhaus K, Ostermann A, Nienhaus GU, Parak FG, Schmidt M Biochemistry. 2005 Apr 5;44(13):5095-105. PMID:15794647<ref>PMID:15794647</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2blh" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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We have determined eight X-ray structures of myoglobin mutant L29W at various experimental conditions. In addition, infrared spectroscopic experiments are presented, which are discussed in the light of the X-ray structures. Two distinct conformations of the CO-ligated protein were identified, giving rise to two stretching bands of heme-bound CO. If L29W MbCO crystals are illuminated around 180 K, a deoxy species is formed. The CO molecules migrate to the proximal side of the heme and remain trapped in the so-called Xe1 cavity upon temperature decrease to 105 K. The structure of this photoproduct is almost identical to the equilibrium high-temperature deoxy Mb structure. If the temperature is cycled to increasingly higher values, CO recombination is observed. Three intermediate structures have been determined during the rebinding process. Efficient recombination occurs only above 180 K, the characteristic temperature for the onset of protein dynamics. Rebinding is remarkably slow because bulky residues His64 and Trp29 block important migration pathways of the CO molecule.
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*[[Myoglobin 3D structures|Myoglobin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2BLH 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=2BLH OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Ligand migration and protein fluctuations in myoglobin mutant L29W., Nienhaus K, Ostermann A, Nienhaus GU, Parak FG, Schmidt M, Biochemistry. 2005 Apr 5;44(13):5095-105. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15794647 15794647]
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[[Category: Physeter catodon]]
[[Category: Physeter catodon]]
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[[Category: Single protein]]
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[[Category: Nienhaus GU]]
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[[Category: Nienhaus, G U.]]
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[[Category: Nienhaus K]]
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[[Category: Nienhaus, K.]]
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[[Category: Ostermann A]]
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[[Category: Ostermann, A.]]
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[[Category: Parak FG]]
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[[Category: Parak, F G.]]
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[[Category: Schmidt M]]
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[[Category: Schmidt, M.]]
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[[Category: heme]]
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[[Category: mutant]]
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[[Category: myoglobin]]
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[[Category: oxygen transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:08:09 2008''
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Current revision

Ligand Migration and Protein Fluctuations in Myoglobin Mutant L29W

PDB ID 2blh

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