2hw4: Difference between revisions

[[Image:2hw4.gif|left|200px]]<br /><applet load="2hw4" size="350" color="white" frame="true" align="right" spinBox="true"  

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.

2HW4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HW4 OCA].  

[[Category: Berg, S Van Den.]]

[[Category: Busam, R D.]]

[[Category: Hallberg, B M.]]

[[Category: SGC, Structural Genomics Consortium.]]

[[Category: Schiavone, L Holmberg.]]

[[Category: Thorsell, A G.]]

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