1V73

Crystal Structure of Cold-Active Protein-Tyrosine Phosphatase of a Psychrophile Shewanella SP.

1V73 の概要

• エントリーDOI: 10.2210/pdb1v73/pdb
• 分子名称: psychrophilic phosphatase I, CALCIUM ION, ACETIC ACID, ... (4 entities in total)
• 機能のキーワード: cold-active enzyme, psychrophile, protein-tyrosine phosphatase, shewanella sp, hydrolase
• 由来する生物種: Shewanella sp.
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38959.11

構造登録者

Tsuruta, H.,Mikami, B.,Aizono, Y. (登録日: 2003-12-09, 公開日: 2005-03-01, 最終更新日: 2024-11-13)

主引用文献

Tsuruta, H.,Mikami, B.,Aizono, Y.
Crystal Structure of Cold-Active Protein-Tyrosine Phosphatase from a Psychrophile, Shewanella sp
J.Biochem.(Tokyo), 137:69-77, 2005

PubMed Abstract: The cold-active protein-tyrosine phosphatase (CAPTPase) of a psychrophile, Shewanella sp., shows high catalytic activity below 20 degrees C. The catalytic residue of CAPTPase is histidine, as opposed to the cysteine of known protein-tyrosine phosphatases (PTPases), and the enzyme protein has three amino acid sequences, Asp-Xaa-His, Gly-Asp-Xaa-Xaa-Asp-Arg and Gly-Asn-His-Glu, that are observed in many protein-serine/threonine phosphatases (PS/TPases). We have determined the crystal structures of CAPTPase at 1.82 angstroms and the enzyme bound with a phosphate ion at 1.90 angstroms resolution using X-ray crystallography and the multiple isomorphous replacement method. The final refined models are comprised of 331 amino acid residues, two metal ions, 447 water molecules, and an acetate or phosphate ion in an asymmetric unit. The enzyme protein consists of three beta-sheets, termed Sheet I, Sheet I', and Sheet II, and 14 alpha-helices. The CAPTPase has a different overall structure from known protein-tyrosine phosphatases. The arrangement of two metal ions, a phosphate ion and the adjacent amino acid residues in the catalytic site of CAPTPase is identical to that of PS/TPases. Thus, it was confirmed that the CAPTPase was a novel PTPase with a conformation similar to the catalytic site of PS/TPase. We speculate that the hydrophobic moiety around the catalytic residue of CAPTPase might play an important role in eliciting high activity at low temperature.

PubMed: 15713885
DOI: 10.1093/jb/mvi010

実験手法

X-RAY DIFFRACTION (1.82 Å)