2HW4

Crystal structure of human phosphohistidine phosphatase

2HW4 の概要

• エントリーDOI: 10.2210/pdb2hw4/pdb
• 分子名称: 14 kDa phosphohistidine phosphatase, FORMIC ACID (3 entities in total)
• 機能のキーワード: phosphohistidine, phosphatase, phpt1, human, structural genomics, structural genomics consortium, sgc, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm (By similarity): Q9NRX4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16951.41

構造登録者

Busam, R.D.,Thorsell, A.G.,Arrowsmith, C.,Berglund, H.,Collins, R.,Edwards, A.,Ehn, M.,Flodin, S.,Flores, A.,Graslund, S.,Hammarstrom, M.,Holmberg Schiavone, L.,Hogbom, M.,Kotenyova, T.,Nilsson-Ehle, P.,Nordlund, P.,Nyman, T.,Ogg, D.,Stenmark, P.,Sundstrom, M.,Uppenberg, J.,Van Den Berg, S.,Weigelt, J.,Persson, C.,Hallberg, B.M.,Structural Genomics Consortium (SGC) (登録日: 2006-07-31, 公開日: 2006-08-29, 最終更新日: 2024-04-03)

主引用文献

Busam, R.D.,Thorsell, A.G.,Flores, A.,Persson, C.,Hallberg, B.M.
First structure of a eukaryotic phosphohistidine phosphatase
J.Biol.Chem., 281:33830-33834, 2006

PubMed Abstract: Phosphatases are a diverse group of enzymes that regulate numerous cellular processes. Much of what is known relates to the tyrosine, threonine, and serine phosphatases, whereas the histidine phosphatases have not been studied as much. The structure of phosphohistidine phosphatase (PHPT1), the first identified eukaryotic-protein histidine phosphatase, has been determined to a resolution of 1.9A using multiple-wavelength anomalous dispersion methods. This enzyme can dephosphorylate a variety of proteins (e.g. ATP-citrate lyase and the beta-subunit of G proteins). A putative active site has been identified by its electrostatic character, ion binding, and conserved protein residues. Histidine 53 is proposed to play a major role in histidine dephosphorylation based on these observations and previous mutational studies. Models of peptide binding are discussed to suggest possible mechanisms for substrate recognition.

PubMed: 16990267
DOI: 10.1074/jbc.C600231200

実験手法

X-RAY DIFFRACTION (1.9 Å)