Cultural advice

The Australian National University acknowledges, celebrates and pays our respects to the Ngunnawal and Ngambri people of the Canberra region and to all First Nations Australians on whose traditional lands we meet and work, and whose cultures are among the oldest continuing cultures in human history.

Aboriginal and Torres Strait Islander peoples are advised that ANU Library collections may include images, names, voices, and other representations of deceased persons.

Material in the collection may contain terms, language or views that reflect the period in which the item was created and may be considered inappropriate today.

The structure and function of a novel glycerophosphodiesterase from Enterobacter aerogenes

Date

Authors

Jackson, Colin

Carr, Paul D

Liu, Jian-Wei

Watt, Stephen J

Beck, Jennifer

Ollis, David

Publisher

Elsevier

Abstract

The structure of the glycerophosphodiesterase (GDPD) from Enterobacter aerogenes, GpdQ, has been solved by SAD phasing from the active site metal ions. Structural analysis indicates that GpdQ belongs to the α/β sandwich metallo-phosphoesterase family, r

Keywords

Keywords: bacterial enzyme; metal ion; metalloprotein; phosphodiesterase; protein GpdQ; protein subunit; unclassified drug; article; beta sheet; controlled study; dimerization; disulfide bond; Enterobacter aerogenes; enzyme active site; enzyme activity; enzyme anal binuclear metallo-enzyme; dynamics; glycerophosphodiester; phosphodiesterase; quaternary structure

URI

http://hdl.handle.net/1885/25546

Collections

ANU Research Publications

Source

Journal of Molecular Biology

Type

Journal article

DOI

10.1016/j.jmb.2007.01.032

Restricted until

2037-12-31

Downloads

File

Description

01_Jackson_The_structure_and_function_of_2007.pdf (2.79 MB)