1myt
From Proteopedia
(New page: 200px<br /><applet load="1myt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1myt, resolution 1.74Å" /> '''CRYSTAL STRUCTURE TO...) |
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| - | [[Image:1myt.gif|left|200px]]<br /><applet load="1myt" size=" | + | [[Image:1myt.gif|left|200px]]<br /><applet load="1myt" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1myt, resolution 1.74Å" /> | caption="1myt, resolution 1.74Å" /> | ||
'''CRYSTAL STRUCTURE TO 1.74 ANGSTROMS RESOLUTION OF METMYOGLOBIN FROM YELLOWFIN TUNA (THUNNUS ALBACARES): AN EXAMPLE OF A MYOGLOBIN LACKING THE D HELIX'''<br /> | '''CRYSTAL STRUCTURE TO 1.74 ANGSTROMS RESOLUTION OF METMYOGLOBIN FROM YELLOWFIN TUNA (THUNNUS ALBACARES): AN EXAMPLE OF A MYOGLOBIN LACKING THE D HELIX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of metmyoglobin from yellowfin tuna (Thunnus | + | The crystal structure of metmyoglobin from yellowfin tuna (Thunnus albacares) has been determined by molecular replacement methods and refined to a conventional R factor of 0.177 for all observed reflections in the range of 6.0-1.70 A resolution. Like other myoglobins for which a high-resolution structure is available, the polypeptide chain is organized into several helices that cooperate to form a hydrophobic pocket into which the heme prosthetic group is non-covalently bound; however, the D helix observed in other myoglobins is absent in myoglobin from yellowfin tuna and has been replaced with a random coil. As well, the A helix has a pronounced kink due to the presence of Pro16. The differences in structure between this and sperm whale myoglobin can be correlated with their reported dioxygen affinity and dissociation. The structure is in agreement with reported fluorescence data which show an increased Trp14.heme distance in yellowfin tuna compared to sperm whale myoglobin. |
==About this Structure== | ==About this Structure== | ||
| - | 1MYT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thunnus_albacares Thunnus albacares] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1MYT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thunnus_albacares Thunnus albacares] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MYT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thunnus albacares]] | [[Category: Thunnus albacares]] | ||
| - | [[Category: Birnbaum, G | + | [[Category: Birnbaum, G I.]] |
| - | [[Category: Evans, S | + | [[Category: Evans, S V.]] |
[[Category: Przybylska, M.]] | [[Category: Przybylska, M.]] | ||
| - | [[Category: Rose, D | + | [[Category: Rose, D R.]] |
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: oxygen transport]] | [[Category: oxygen transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:00:27 2008'' |
Revision as of 12:00, 21 February 2008
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CRYSTAL STRUCTURE TO 1.74 ANGSTROMS RESOLUTION OF METMYOGLOBIN FROM YELLOWFIN TUNA (THUNNUS ALBACARES): AN EXAMPLE OF A MYOGLOBIN LACKING THE D HELIX
Overview
The crystal structure of metmyoglobin from yellowfin tuna (Thunnus albacares) has been determined by molecular replacement methods and refined to a conventional R factor of 0.177 for all observed reflections in the range of 6.0-1.70 A resolution. Like other myoglobins for which a high-resolution structure is available, the polypeptide chain is organized into several helices that cooperate to form a hydrophobic pocket into which the heme prosthetic group is non-covalently bound; however, the D helix observed in other myoglobins is absent in myoglobin from yellowfin tuna and has been replaced with a random coil. As well, the A helix has a pronounced kink due to the presence of Pro16. The differences in structure between this and sperm whale myoglobin can be correlated with their reported dioxygen affinity and dissociation. The structure is in agreement with reported fluorescence data which show an increased Trp14.heme distance in yellowfin tuna compared to sperm whale myoglobin.
About this Structure
1MYT is a Single protein structure of sequence from Thunnus albacares with as ligand. Full crystallographic information is available from OCA.
Reference
1.70 A resolution structure of myoglobin from yellowfin tuna. An example of a myoglobin lacking the D helix., Birnbaum GI, Evans SV, Przybylska M, Rose DR, Acta Crystallogr D Biol Crystallogr. 1994 May 1;50(Pt 3):283-9. PMID:15299440
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