1dws
From Proteopedia
(New page: 200px<br /><applet load="1dws" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dws, resolution 1.45Å" /> '''PHOTOLYZED CARBONMON...) |
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| - | [[Image:1dws.gif|left|200px]]<br /><applet load="1dws" size=" | + | [[Image:1dws.gif|left|200px]]<br /><applet load="1dws" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dws, resolution 1.45Å" /> | caption="1dws, resolution 1.45Å" /> | ||
'''PHOTOLYZED CARBONMONOXY MYOGLOBIN (HORSE HEART)'''<br /> | '''PHOTOLYZED CARBONMONOXY MYOGLOBIN (HORSE HEART)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Small molecules such as NO, O2, CO or H2 are important biological ligands | + | 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== | ==About this Structure== | ||
| - | 1DWS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with SO4, HEM and CMO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1DWS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=CMO:'>CMO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DWS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Berendzen, J.]] | [[Category: Berendzen, J.]] | ||
[[Category: Chu, K.]] | [[Category: Chu, K.]] | ||
| - | [[Category: Mcmahon, B | + | [[Category: Mcmahon, B H.]] |
[[Category: Schlichting, I.]] | [[Category: Schlichting, I.]] | ||
| - | [[Category: Sweet, R | + | [[Category: Sweet, R M.]] |
[[Category: Vojtechovsky, J.]] | [[Category: Vojtechovsky, J.]] | ||
[[Category: CMO]] | [[Category: CMO]] | ||
| Line 25: | Line 25: | ||
[[Category: respiratory protein]] | [[Category: respiratory protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:21:24 2008'' |
Revision as of 10:21, 21 February 2008
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PHOTOLYZED CARBONMONOXY MYOGLOBIN (HORSE HEART)
Overview
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
1DWS is a Single protein structure of sequence from Equus caballus with , and as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 12:21:24 2008
