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1s3p

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[[Image:1s3p.jpg|left|200px]]<br /><applet load="1s3p" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1s3p.jpg|left|200px]]
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caption="1s3p, resolution 2.00&Aring;" />
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'''Crystal structure of rat alpha-parvalbumin S55D/E59D mutant'''<br />
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{{Structure
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|PDB= 1s3p |SIZE=350|CAPTION= <scene name='initialview01'>1s3p</scene>, resolution 2.00&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</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 S55D/E59D mutant'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1S3P 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> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S3P OCA].
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1S3P 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=1S3P OCA].
==Reference==
==Reference==
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Crystal structure of a high-affinity variant of rat alpha-parvalbumin., Lee YH, Tanner JJ, Larson JD, Henzl MT, Biochemistry. 2004 Aug 10;43(31):10008-17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15287728 15287728]
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Crystal structure of a high-affinity variant of rat alpha-parvalbumin., Lee YH, Tanner JJ, Larson JD, Henzl MT, Biochemistry. 2004 Aug 10;43(31):10008-17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15287728 15287728]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: parvalbumin]]
[[Category: parvalbumin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:57:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:00:05 2008''

Revision as of 12:00, 20 March 2008


PDB ID 1s3p

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: and
Gene: PVALB, PVA (Rattus norvegicus)
Coordinates: save as pdb, mmCIF, xml



Crystal structure of rat alpha-parvalbumin S55D/E59D mutant


Overview

In model peptide systems, Ca2+ affinity is maximized in EF-hand motifs containing four carboxylates positioned on the +x and -x and +z and -z axes; introduction of a fifth carboxylate ligand reduces the affinity. However, in rat beta-parvalbumin, replacement of Ser-55 with aspartate heightens divalent ion affinity [Henzl, M. T., et al. (1996) Biochemistry 35, 5856-5869]. The corresponding alpha-parvalbumin variant (S55D/E59D) likewise exhibits elevated affinity [Henzl, M. T., et al. (2003) Anal. Biochem. 319, 216-233]. To determine whether these mutations produce a variation on the archetypal EF-hand coordination scheme, we have obtained high-resolution X-ray crystallographic data for alpha S55D/E59D. As anticipated, the aspartyl carboxylate replaces the serine hydroxyl at the +z coordination position. Interestingly, the Asp-59 carboxylate abandons the role it plays as an outer sphere ligand in wild-type rat beta, rotating away from the Ca2+ and, instead, forming a hydrogen bond with the amide of Glu-62. Superficially, the coordination sphere in the CD site of alpha S55D/E59D resembles that in the EF site. However, the orientation of the Asp-59 side chain is predicted to stabilize the D-helix, which may contribute to the heightened divalent ion affinity. DSC data indicate that the alpha S55D/E59D variant retains the capacity to bind 1 equiv of Na+. Consistent with this finding, when binding measurements are conducted in K(+)-containing buffer, divalent ion affinity is markedly higher. In 0.15 M KCl and 0.025 M Hepes-KOH (pH 7.4) at 5 degrees C, the macroscopic Ca2+ binding constants are 1.8 x 10(10) and 2.0 x 10(9) M(-1). The corresponding Mg2+ binding constants are 2.7 x 10(6) and 1.2 x 10(5) M(-1).

About this Structure

1S3P is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structure of a high-affinity variant of rat alpha-parvalbumin., Lee YH, Tanner JJ, Larson JD, Henzl MT, Biochemistry. 2004 Aug 10;43(31):10008-17. PMID:15287728

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