Structural and biochemical characterization of a halophilic archaeal alkaline phosphatase

Andy Wende, Patrik Johansson, Ronnald Vollrath, Michael Dyall-Smith, Dieter Oesterhelt, Martin Grininger

Research output: Contribution to journalArticlepeer-review

20 Citations (Scopus)


Phosphate is an essential component of all cells that must be taken up from the environment. Prokaryotes commonly secrete alkaline phosphatases (APs) to recruit phosphate from organic compounds by hydrolysis. In this study, the AP from Halobacterium salinarum, an archaeon that lives in a saturated salt environment, has been functionally and structurally characterized. The core fold and the active-site architecture of the H. salinarum enzyme are similar to other AP structures. These generally form dimers composed of dominant beta-sheet structures sandwiched by alpha-helices and have well-accessible active sites. The surface of the enzyme is predicted to be highly negatively charged, like other proteins of extreme halophiles. In addition to the conserved core, most APs contain a crown domain that strongly varies within species. In the H. salinarum AP, the crown domain is made of an acyl-carrier-protein-like fold. Different from other APs, it is not involved in dimer formation. We compare the archaeal AP with its bacterial and eukaryotic counterparts, and we focus on the role of crown domains in enhancing protein stability, regulating enzyme function, and guiding phosphoesters into the active-site funnel
Original languageEnglish
Pages (from-to)52-62
Number of pages11
JournalJournal of Molecular Biology
Issue number1
Publication statusPublished - Jul 2010


Dive into the research topics of 'Structural and biochemical characterization of a halophilic archaeal alkaline phosphatase'. Together they form a unique fingerprint.

Cite this