Reports summarize enzyme research study results from RIKEN

New research, 'Crystal structure of monofunctional histidinol phosphate phosphatase from Thermus thermophilus HB8,' is the subject of a report. "Monofunctional histidinol phosphate phosphatase from Thermus thermophilus HB8, which catalyzes the dephosphorylation of l-histidinol phosphate, belongs to the PHP family, together with the PHP domain of bacterial DNA polymerase III and family X DNA polymerase. We have determined the structures of the complex with a sulfate ion, the complex with a phosphate ion, and the unliganded form at 1.6, 2.1, and 1.8 A resolution, respectively," investigators in Sayo, Japan report.

"The enzyme exists as a tetramer, and the subunit consists...

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