1ue8: Difference between revisions

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New page: left|200px<br /><applet load="1ue8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ue8, resolution 3.00Å" /> '''Crystal Structure of...
 
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[[Image:1ue8.jpg|left|200px]]<br /><applet load="1ue8" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ue8.jpg|left|200px]]<br /><applet load="1ue8" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ue8, resolution 3.00&Aring;" />
caption="1ue8, resolution 3.00&Aring;" />
'''Crystal Structure of Thermophilic Cytochrome P450 from Sulfolobus tokodaii'''<br />
'''Crystal Structure of Thermophilic Cytochrome P450 from Sulfolobus tokodaii'''<br />


==Overview==
==Overview==
Cytochrome P450 from thermoacidophilic crenarchaeon, Sulfolobus tokodaii, strain 7 (P450st) has been expressed in Escherichia coli and purified at, high homogeneity. P450st was crystallized in an orthorhombic system with, the space group P2(1)2(1)2(1) and cell dimensions of a=53.6 A, b=55.1 A, and c=130.9 A, and the structure was determined at a 3.0 A resolution. The, final R-factor was 0.194 (Rfree=0.235). Structural comparison with, cytochrome P450 from S. solfataricus (CYP119) suggests that the region, composed of the F to G helices and the Cl- binding site is responsible for, the affinity for a ligand coordinating heme iron. Direct electrochemistry, of P450st in a didodecyldimethylammonium bromide (DDAB) film on a plastic, formed carbon (PFC) electrode has also been demonstrated. A, quasi-reversible redox response has been observed even at elevated, temperatures of up to 80 degrees C.
Cytochrome P450 from thermoacidophilic crenarchaeon, Sulfolobus tokodaii strain 7 (P450st) has been expressed in Escherichia coli and purified at high homogeneity. P450st was crystallized in an orthorhombic system with the space group P2(1)2(1)2(1) and cell dimensions of a=53.6 A, b=55.1 A, and c=130.9 A, and the structure was determined at a 3.0 A resolution. The final R-factor was 0.194 (Rfree=0.235). Structural comparison with cytochrome P450 from S. solfataricus (CYP119) suggests that the region composed of the F to G helices and the Cl- binding site is responsible for the affinity for a ligand coordinating heme iron. Direct electrochemistry of P450st in a didodecyldimethylammonium bromide (DDAB) film on a plastic formed carbon (PFC) electrode has also been demonstrated. A quasi-reversible redox response has been observed even at elevated temperatures of up to 80 degrees C.


==About this Structure==
==About this Structure==
1UE8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_tokodaii Sulfolobus tokodaii] with CL and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UE8 OCA].  
1UE8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_tokodaii Sulfolobus tokodaii] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UE8 OCA].  


==Reference==
==Reference==
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[[Category: structural genomics]]
[[Category: structural genomics]]


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