1rwy

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[[Image:1rwy.gif|left|200px]]<br /><applet load="1rwy" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rwy.gif|left|200px]]
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caption="1rwy, resolution 1.05&Aring;" />
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'''CRYSTAL STRUCTURE OF RAT ALPHA-PARVALBUMIN AT 1.05 RESOLUTION'''<br />
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{{Structure
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|PDB= 1rwy |SIZE=350|CAPTION= <scene name='initialview01'>1rwy</scene>, resolution 1.05&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene>
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|ACTIVITY=
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|GENE= PVALB, PVA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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}}
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'''CRYSTAL STRUCTURE OF RAT ALPHA-PARVALBUMIN AT 1.05 RESOLUTION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1RWY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=NH4:'>NH4</scene>, <scene name='pdbligand=PG4:'>PG4</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RWY OCA].
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1RWY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RWY OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15169955 15169955]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15169955 15169955]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: ef-hand]]
[[Category: ef-hand]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:57:20 2008''

Revision as of 11:57, 20 March 2008

Image:1rwy.gif


PDB ID 1rwy

Drag the structure with the mouse to rotate
, resolution 1.05Å
Ligands: , , , and
Gene: PVALB, PVA (Rattus norvegicus)
Coordinates: save as pdb, mmCIF, xml



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. 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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