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1mz0: Difference between revisions

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<StructureSection load='1mz0' size='340' side='right'caption='[[1mz0]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='1mz0' size='340' side='right'caption='[[1mz0]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mz0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phymc Phymc]. 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>
<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>
</td></tr><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>
</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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dxc|1dxc]], [[1myz|1myz]]</div></td></tr>
<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>
<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>
<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>
</table>
</table>
== Function ==
== Function ==
[[https://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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:12847289<ref>PMID:12847289</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1mz0" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Phymc]]
[[Category: Physeter catodon]]
[[Category: Anfinrud, P]]
[[Category: Anfinrud P]]
[[Category: Arcovito, A]]
[[Category: Arcovito A]]
[[Category: Bourgeois, D]]
[[Category: Bourgeois D]]
[[Category: Brunori, M]]
[[Category: Brunori M]]
[[Category: Miele, A E]]
[[Category: Miele AE]]
[[Category: Schotte, F]]
[[Category: Schotte F]]
[[Category: Sciara, G]]
[[Category: Sciara G]]
[[Category: Vallone, B]]
[[Category: Vallone B]]
[[Category: Wulff, M]]
[[Category: Wulff M]]
[[Category: Co complex]]
[[Category: Heme]]
[[Category: Oxygen storage]]
[[Category: Oxygen storage-transport complex]]
[[Category: Respiratory protein]]

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