1RTP

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

1RTP の概要

• エントリーDOI: 10.2210/pdb1rtp/pdb
• 分子名称: ALPHA-PARVALBUMIN, CALCIUM ION (3 entities in total)
• 機能のキーワード: calcium-binding protein
• 由来する生物種: Rattus rattus (black rat)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 35680.49

構造登録者

Mcphalen, C.A.,Sielecki, A.R.,Santarsiero, B.D.,James, M.N.G. (登録日: 1993-05-14, 公開日: 1994-01-31, 最終更新日: 2024-02-14)

主引用文献

McPhalen, C.A.,Sielecki, A.R.,Santarsiero, B.D.,James, M.N.
Refined crystal structure of rat parvalbumin, a mammalian alpha-lineage parvalbumin, at 2.0 A resolution.
J.Mol.Biol., 235:718-732, 1994

PubMed Abstract: 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.

PubMed: 8289291
DOI: 10.1006/jmbi.1994.1023

実験手法

X-RAY DIFFRACTION (2 Å)