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| - | [[Image:1rwy.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1rwy| PDB=1rwy | SCENE= }} | | {{STRUCTURE_1rwy| PDB=1rwy | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF RAT ALPHA-PARVALBUMIN AT 1.05 RESOLUTION'''
| + | ===CRYSTAL STRUCTURE OF RAT ALPHA-PARVALBUMIN AT 1.05 RESOLUTION=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15169955}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15169955 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15169955}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Calcium-binding]] | | [[Category: Calcium-binding]] |
| | [[Category: Ef-hand]] | | [[Category: Ef-hand]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:00:20 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:19:45 2008'' |
Revision as of 02:19, 28 July 2008
Template:STRUCTURE 1rwy
CRYSTAL STRUCTURE OF RAT ALPHA-PARVALBUMIN AT 1.05 RESOLUTION
Template:ABSTRACT PUBMED 15169955
About this Structure
1RWY is a Single protein structure of sequence from Rattus norvegicus. 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
Page seeded by OCA on Mon Jul 28 05:19:45 2008
