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[[Image:1dwt.gif|left|200px]]
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{{STRUCTURE_1dwt|  PDB=1dwt  |  SCENE=  }}
'''PHOTORELAXED HORSE HEART MYOGLOBIN CO COMPLEX'''


==Photorelaxed horse heart MYOGLOBIN CO complex==
<StructureSection load='1dwt' size='340' side='right'caption='[[1dwt]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1dwt]] 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=1DWT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DWT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</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=1dwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dwt OCA], [https://pdbe.org/1dwt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dwt RCSB], [https://www.ebi.ac.uk/pdbsum/1dwt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dwt ProSAT]</span></td></tr>
</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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dw/1dwt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1dwt ConSurf].
<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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1DWT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DWT OCA].
</div>
<div class="pdbe-citations 1dwt" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/10706294 10706294]
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Berendzen, J.]]
[[Category: Berendzen J]]
[[Category: Chu, K.]]
[[Category: Chu K]]
[[Category: Mcmahon, B H.]]
[[Category: McMahon BH]]
[[Category: Schlichting, I.]]
[[Category: Schlichting I]]
[[Category: Sweet, R M.]]
[[Category: Sweet RM]]
[[Category: Vojtechovsky, J.]]
[[Category: Vojtechovsky J]]
[[Category: Oxygen transport]]
[[Category: Respiratory protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:22:33 2008''
Retrieved from "https://proteopedia.org/1dwt"