1RJV

Solution Structure of Human alpha-Parvalbumin refined with a paramagnetism-based strategy

Summary for 1RJV

• Entry DOI: 10.2210/pdb1rjv/pdb
• Descriptor: Parvalbumin alpha, CALCIUM ION (2 entities in total)
• Functional Keywords: calcium, parvalbumin, ef-hand, lanthanide, structural proteomics in europe, spine, structural genomics, metal binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 12157.93

Authors

Baig, I.,Bertini, I.,Del Bianco, C.,Gupta, Y.K.,Lee, Y.M.,Luchinat, C.,Quattrone, A.,Structural Proteomics in Europe (SPINE) (deposition date: 2003-11-20, release date: 2004-05-25, Last modification date: 2024-05-22)

Primary citation

Baig, I.,Bertini, I.,Del Bianco, C.,Gupta, Y.K.,Lee, Y.M.,Luchinat, C.,Quattrone, A.
Paramagnetism-Based Refinement Strategy for the Solution Structure of Human alpha-Parvalbumin.
Biochemistry, 43:5562-5573, 2004

PubMed Abstract: In the frame of a research aimed at the detailed structural characterization of human calcium-binding proteins of the EF-hand family, the solution structure of human alpha-parvalbumin has been solved by NMR and refined with the help of substitution of the Ca(2+) ion in the EF site with the paramagnetic Dy(3+) ion. A simple (1)H-(15)N HSQC spectrum allowed the NH assignments based on the properties of Dy(3+). This allowed us to exploit pseudocontact shifts and residual dipolar couplings for solution structure refinement. The backbone and heavy atom RMSD are 0.55 +/- 0.08 and 1.02 +/- 0.08 A, respectively, and decrease to 0.39 +/- 0.05 and 0.90 +/- 0.06 A upon refinement with paramagnetism-based restraints. The RMSD for the metal itself in the EF site in the refined structure is 0.26 +/- 0.12 A. Backbone NH R(1), R(2), and NOE measured at two temperatures show the protein to be relatively rigid. The NH orientations are well determined by the paramagnetism-based restraints. This allows us to detect small but significant local structural differences with the orthologue protein from rat, whose X-ray structure is available at 2.0 A resolution. All differences are related to local changes in the amino acidic composition.

PubMed: 15122922
DOI: 10.1021/bi035879k

Experimental method

SOLUTION NMR