1mz0

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(New page: 200px<br /><applet load="1mz0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mz0, resolution 1.60&Aring;" /> '''STRUCTURE OF MYOGLOB...)
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[[Image:1mz0.jpg|left|200px]]<br /><applet load="1mz0" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mz0, resolution 1.60&Aring;" />
 
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'''STRUCTURE OF MYOGLOBIN MB-YQR 316 ns AFTER PHOTOLYSIS OF CARBON MONOXIDE SOLVED FROM LAUE DATA AT RT.'''<br />
 
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==Overview==
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==STRUCTURE OF MYOGLOBIN MB-YQR 316 ns AFTER PHOTOLYSIS OF CARBON MONOXIDE SOLVED FROM LAUE DATA AT RT.==
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Although conformational changes are essential for the function of, proteins, little is known about their structural dynamics at atomic level, resolution. Myoglobin (Mb) is the paradigm to investigate conformational, dynamics because it is a simple globular heme protein displaying a, photosensitivity of the iron-ligand bond. Upon laser photodissociation of, carboxymyoglobin Mb a nonequilibrium population of protein structures is, generated that relaxes over a broad time range extending from picoseconds, to milliseconds. This process is associated with migration of the ligand, to cavities in the matrix and with a reduction in the geminate rebinding, rate by several orders of magnitude. Here we report nanosecond, time-resolved Laue diffraction data to 1.55-A resolution on a Mb mutant, which depicts the sequence of structural events associated with this, extended relaxation. Motions of the distal E-helix, including the mutated, residue Gln-64(E7), and of the CD-turn are found to lag significantly, (100-300 ns) behind local rearrangements around the heme such as heme, tilting, iron motion out of the heme plane, and swinging of the mutated, residue Tyr-29(B10), all of which occur promptly (&lt; or =3 ns). Over the, same delayed time range, CO is observed to migrate from a cavity distal to, the heme known to bind xenon (called Xe4) to another such cavity proximal, to the heme (Xe1). We propose that the extended relaxation of the globin, moiety reflects reequilibration among conformational substates known to, play an essential role in controlling protein function.
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<StructureSection load='1mz0' size='340' side='right'caption='[[1mz0]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mz0]] 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=1MZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MZ0 FirstGlance]. <br>
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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]] 1.6&#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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mz0 OCA], [https://pdbe.org/1mz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mz0 RCSB], [https://www.ebi.ac.uk/pdbsum/1mz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mz0 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/mz/1mz0_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=1mz0 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1MZ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with SO4, HEM and CMO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MZ0 OCA].
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*[[Myoglobin 3D structures|Myoglobin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Complex landscape of protein structural dynamics unveiled by nanosecond Laue crystallography., Bourgeois D, Vallone B, Schotte F, Arcovito A, Miele AE, Sciara G, Wulff M, Anfinrud P, Brunori M, Proc Natl Acad Sci U S A. 2003 Jul 22;100(15):8704-9. Epub 2003 Jul 7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12847289 12847289]
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[[Category: Large Structures]]
[[Category: Physeter catodon]]
[[Category: Physeter catodon]]
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[[Category: Single protein]]
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[[Category: Anfinrud P]]
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[[Category: Anfinrud, P.]]
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[[Category: Arcovito A]]
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[[Category: Arcovito, A.]]
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[[Category: Bourgeois D]]
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[[Category: Bourgeois, D.]]
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[[Category: Brunori M]]
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[[Category: Brunori, M.]]
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[[Category: Miele AE]]
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[[Category: Miele, A.E.]]
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[[Category: Schotte F]]
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[[Category: Schotte, F.]]
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[[Category: Sciara G]]
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[[Category: Sciara, G.]]
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[[Category: Vallone B]]
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[[Category: Vallone, B.]]
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[[Category: Wulff M]]
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[[Category: Wulff, M.]]
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[[Category: CMO]]
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[[Category: HEM]]
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[[Category: SO4]]
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[[Category: co complex]]
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[[Category: heme]]
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[[Category: oxygen storage]]
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[[Category: respiratory protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:49:21 2007''
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Current revision

STRUCTURE OF MYOGLOBIN MB-YQR 316 ns AFTER PHOTOLYSIS OF CARBON MONOXIDE SOLVED FROM LAUE DATA AT RT.

PDB ID 1mz0

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