1bvc
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(New page: 200px<br /><applet load="1bvc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bvc, resolution 1.5Å" /> '''STRUCTURE OF A BILIVE...)
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Revision as of 09:49, 20 November 2007
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STRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM D) AT 118 K
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.
About this Structure
1BVC is a Single protein structure of sequence from Physeter catodon with PO4 and BLA as ligands. Full crystallographic information is available from OCA.
Reference
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
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