2HW4

Crystal structure of human phosphohistidine phosphatase

Summary for 2HW4

• Entry DOI: 10.2210/pdb2hw4/pdb
• Descriptor: 14 kDa phosphohistidine phosphatase, FORMIC ACID (3 entities in total)
• Functional Keywords: phosphohistidine, phosphatase, phpt1, human, structural genomics, structural genomics consortium, sgc, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm (By similarity): Q9NRX4
• Total number of polymer chains: 1
• Total formula weight: 16951.41

Authors

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) (deposition date: 2006-07-31, release date: 2006-08-29, Last modification date: 2024-04-03)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)