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1rwy

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(New page: 200px<br /><applet load="1rwy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rwy, resolution 1.05&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 23:47, 20 November 2007

Image:1rwy.gif

1rwy, resolution 1.05Å

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CRYSTAL STRUCTURE OF RAT ALPHA-PARVALBUMIN AT 1.05 RESOLUTION

Overview

The crystal structure of rat alpha-parvalbumin has been determined at 1.05, Angstrom resolution, using synchrotron data collected at Advanced Photon, Source beamline 19-ID. After refinement with SHELX, employing anisotropic, displacement parameters and riding hydrogen atoms, R = 0.132 and R(free) =, 0.162. The average coordinate estimated standard deviations are 0.021, Angstrom and 0.038 Angstrom for backbone atoms and side-chain atoms, respectively. Besides providing a more precise view of the alpha-isoform, than previously available, these data permit comparison with the 0.91, Angstrom structure determined for pike beta-parvalbumin. Visualization of, the anisotropic displacement parameters as thermal ellipsoids yields, insight into the atomic motion within the Ca(2+)-binding sites. The, asymmetric unit includes three parvalbumin (PV) molecules. Interestingly, the EF site in one displays uncharacteristic flexibility. The ellipsoids, for Asp-92 are particularly large and non-spherical, and the shape of the, Ca(2+) ellipsoid implies significant vibrational motion perpendicular to, the plane defined by the four y and z ligands. The relative dearth of, crystal-packing interactions in this site suggests that the heightened, flexibility may be the result of diminished intermolecular contacts. The, implication is that, by impeding conformational mobility, crystal-packing, forces may cause serious overestimation of EF-hand rigidity. The high, quality of the data permitted 11 residues to be modeled in alternative, side-chain conformations, including the two core residues, Ile-97 and, Leu-105. The discrete disorder observed for Ile-97 may have functional, ramifications, providing a mechanism for communicating binding status, between the CD and EF binding loops and between the PV metal ion-binding, domain and the N-terminal AB region.

About this Structure

1RWY is a Single protein structure of sequence from Rattus norvegicus with CA, SO4, NH4, PG4 and ACY as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of rat alpha-parvalbumin at 1.05 Angstrom resolution., Bottoms CA, Schuermann JP, Agah S, Henzl MT, Tanner JJ, Protein Sci. 2004 Jul;13(7):1724-34. Epub 2004 May 28. PMID:15169955

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