1s3p
From Proteopedia
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'''Crystal structure of rat alpha-parvalbumin S55D/E59D mutant''' | '''Crystal structure of rat alpha-parvalbumin S55D/E59D mutant''' | ||
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[[Category: Henzl, M T.]] | [[Category: Henzl, M T.]] | ||
[[Category: Tanner, J J.]] | [[Category: Tanner, J J.]] | ||
| - | [[Category: | + | [[Category: Calcium-binding protein]] |
| - | [[Category: | + | [[Category: Ef-hand]] |
| - | [[Category: | + | [[Category: Parvalbumin]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:15:37 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 05:15, 3 May 2008
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 Page seeded by OCA on Sat May 3 08:15:37 2008
