1bvc: Difference between revisions

Revision as of 12:59, 21 February 2008

STRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM D) AT 118 K

OverviewOverview

Crystal structure determinations of two orthorhombic (P2(1)2(1)2(1)) crystal modifications of the biliverdin apomyoglobin complex are described. The two structures were determined by X-ray diffraction at 100 K to a resolution of 1.5 A and 1.4 A. Both crystal forms were grown by hanging-drop techniques, using phosphate as precipitant. The structures were solved by molecular replacement and refined to final R-values of 19.4% and 21.2%. Both structures are very similar with respect to the binding site and the conformation of the biliverdin chromophore, which occurs in a (P) helical conformation. It is located within the heme pocket, very close in position and orientation to the heme binding site in myoglobin. Two water molecules not present in the crystal structure of myoglobin are sequestered within the heme pocket in the biliverdin-apomyoglobin complex, and they are engaged in hydrogen bonding to the biliverdin and to the protein. Comparison with structural results from an earlier NMR study of the same complex shows good agreement.

About this StructureAbout this Structure

1BVC is a Single protein structure of sequence from Physeter catodon with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Structure determination of the biliverdin apomyoglobin complex: crystal structure analysis of two crystal forms at 1.4 and 1.5 A resolution., Wagner UG, Muller N, Schmitzberger W, Falk H, Kratky C, J Mol Biol. 1995 Mar 24;247(2):326-37. PMID:7707378

Page seeded by OCA on Thu Feb 21 11:59:29 2008

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OCA

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-[[Image:1bvc.gif|left|200px]]<br /><applet load="1bvc" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1bvc.gif|left|200px]]<br /><applet load="1bvc" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1bvc, resolution 1.5&Aring;" />
 '''STRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM D) AT 118 K'''<br />
 ==Overview==
-Crystal structure determinations of two orthorhombic (P2(1)2(1)2(1)), crystal modifications of the biliverdin apomyoglobin complex are, described. The two structures were determined by X-ray diffraction at 100, K to a resolution of 1.5 A and 1.4 A. Both crystal forms were grown by, hanging-drop techniques, using phosphate as precipitant. The structures, were solved by molecular replacement and refined to final R-values of, 19.4% and 21.2%. Both structures are very similar with respect to the, binding site and the conformation of the biliverdin chromophore, which, occurs in a (P) helical conformation. It is located within the heme, pocket, very close in position and orientation to the heme binding site in, myoglobin. Two water molecules not present in the crystal structure of, myoglobin are sequestered within the heme pocket in the, biliverdin-apomyoglobin complex, and they are engaged in hydrogen bonding, to the biliverdin and to the protein. Comparison with structural results, from an earlier NMR study of the same complex shows good agreement.
+Crystal structure determinations of two orthorhombic (P2(1)2(1)2(1)) crystal modifications of the biliverdin apomyoglobin complex are described. The two structures were determined by X-ray diffraction at 100 K to a resolution of 1.5 A and 1.4 A. Both crystal forms were grown by hanging-drop techniques, using phosphate as precipitant. The structures were solved by molecular replacement and refined to final R-values of 19.4% and 21.2%. Both structures are very similar with respect to the binding site and the conformation of the biliverdin chromophore, which occurs in a (P) helical conformation. It is located within the heme pocket, very close in position and orientation to the heme binding site in myoglobin. Two water molecules not present in the crystal structure of myoglobin are sequestered within the heme pocket in the biliverdin-apomyoglobin complex, and they are engaged in hydrogen bonding to the biliverdin and to the protein. Comparison with structural results from an earlier NMR study of the same complex shows good agreement.
 ==About this Structure==
-BVC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with PO4 and BLA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BVC OCA].
+BVC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=BLA:'>BLA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BVC OCA].
 ==Reference==
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 [[Category: Mueller, N.]]
 [[Category: Schmitzberger, W.]]
-[[Category: Wagner, U.G.]]
+[[Category: Wagner, U G.]]
 [[Category: BLA]]
 [[Category: PO4]]
 [[Category: oxygen storage]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:56:59 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:29 2008''