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1rtp

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Image:1rtp.jpg

1rtp, resolution 2.0Å

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REFINED X-RAY STRUCTURE OF RAT PARVALBUMIN, A MAMMALIAN ALPHA-LINEAGE PARVALBUMIN, AT 2.0 A RESOLUTION

Overview

We present here the X-ray crystal structure of the rat alpha-parvalbumin, from fast twitch muscle. This protein (M(r) 11.8 kDa) crystallizes in, space group P2(1)2(1)2(1) with unit cell dimensions of a = 34.3 A, b =, 55.0 A, c = 156.1 A and three molecules in the asymmetric unit. The, protein structure was solved by the molecular replacement method and has, been refined to a crystallographic R-factor [formula: see text] of 0.181, for all reflections with I/sigma(I) > or = 2 (I = intensity) between 8.0, and 2.0 A resolution. The molecules located most easily in the molecular, replacement rotation function had lower overall thermal motion parameters, and higher numbers of intermolecular crystal packing contacts. The overall, fold of the polypeptide chain for the rat alpha-parvalbumin is similar to, other known parvalbumin structures (root-mean-square deviations in, alpha-carbon atom positions range from 0.60 to 0.87 A). There are two, Ca(2+)-binding sites in parvalbumins, and there is some evidence for a, third ion-binding site, adjacent to the CD site, in the rat species. The, level of structural variability among the best-ordered regions of the, three independent rat alpha-parvalbumin molecules in the crystallographic, asymmetric unit is two to three times higher than the mean coordinate, error (0.10 A), indicating flexibility in the molecule. Sequence, differences between alpha and beta-lineage parvalbumins result in, repacking of the hydrophobic core and some shifts in the protein backbone., The shifts are localized, however, and entire helices do not shift as, rigid units.

About this Structure

1RTP is a Single protein structure of sequence from Rattus rattus with CA as ligand. Full crystallographic information is available from OCA.

Reference

Refined crystal structure of rat parvalbumin, a mammalian alpha-lineage parvalbumin, at 2.0 A resolution., McPhalen CA, Sielecki AR, Santarsiero BD, James MN, J Mol Biol. 1994 Jan 14;235(2):718-32. PMID:8289291

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