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==== | ==PHOTOLYZED CARBONMONOXY MYOGLOBIN (HORSE HEART)== | ||
<StructureSection load='1dws' size='340' side='right'caption='[[1dws]]' scene=''> | <StructureSection load='1dws' size='340' side='right'caption='[[1dws]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[1dws]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DWS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DWS FirstGlance]. <br> | ||
</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=1dws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dws OCA], [https://pdbe.org/1dws PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dws RCSB], [https://www.ebi.ac.uk/pdbsum/1dws PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dws ProSAT]</span></td></tr> | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dwr|1dwr]], [[1dwt|1dwt]], [[1azi|1azi]], [[1yma|1yma]], [[1ymb|1ymb]], [[1ymc|1ymc]], [[1hrm|1hrm]], [[1hsy|1hsy]], [[1rse|1rse]], [[1xch|1xch]], [[1wla|1wla]], [[1bje|1bje]]</div></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=1dws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dws OCA], [https://pdbe.org/1dws PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dws RCSB], [https://www.ebi.ac.uk/pdbsum/1dws PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dws ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE]] 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=1dws 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=1dws ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Small molecules such as NO, O2, CO or H2 are important biological ligands that bind to metalloproteins to function crucially in processes such as signal transduction, respiration and catalysis. A key issue for understanding the regulation of reaction mechanisms in these systems is whether ligands gain access to the binding sites through specific channels and docking sites, or by random diffusion through the protein matrix. A model system for studying this issue is myoglobin, a simple haem protein. Myoglobin has been studied extensively by spectroscopy, crystallography, computation and theory. It serves as an aid to oxygen diffusion but also binds carbon monoxide, a byproduct of endogenous haem catabolism. Molecular dynamics simulations, random mutagenesis and flash photolysis studies indicate that ligand migration occurs through a limited number of pathways involving docking sites. Here we report the 1.4 A resolution crystal structure of a ligand-binding intermediate in carbonmonoxy myoglobin that may have far-reaching implications for understanding the dynamics of ligand binding and catalysis. | |||
Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobin.,Chu K, Vojtchovsky J, McMahon BH, Sweet RM, Berendzen J, Schlichting I Nature. 2000 Feb 24;403(6772):921-3. PMID:10706294<ref>PMID:10706294</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1dws" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Myoglobin 3D structures|Myoglobin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Equus caballus]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Berendzen, J]] | ||
[[Category: Chu, K]] | |||
[[Category: McMahon, B H]] | |||
[[Category: Schlichting, I]] | |||
[[Category: Sweet, R M]] | |||
[[Category: Vojtechovsky, J]] | |||
[[Category: Oxygen transport]] | |||
[[Category: Respiratory protein]] | |||