Department of Biochemistry University of Oxford Department of Biochemistry
University of Oxford
South Parks Road
Oxford OX1 3QU

Tel: +44 (0)1865 613200
Fax: +44 (0)1865 613201
Collage of Drosophila third instar larva optic lobe
Lu Yang, Davis lab
First year Biochemistry students at a practical class
Image showing the global movement of lipids in a model planar membrane
Matthieu Chavent, Sansom lab
Anaphase bridges in fission yeast cells
Whitby lab
Lactose permease represented using bending cylinders in Bendix software
Caroline Dahl, Sansom lab
Epithelial cells in C. elegans showing a seam cell that failed to undergo cytokinesis
Serena Ding, Woollard lab
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News

A new class of ion pump inhibitors could help fight infectious fungi
A) Cartoon representation of the Ca2+-pump bound to a HyC (labeled 7). Pump domains and ligands are indicated. The bound HyC and ATP analogue TNPATP are shown as sticks (C: yellow or marine, O: red, Br: dark red, F: pale cyan, N: blue, P: orange) B) Sliced surface view revealing the the ligand-binding pocket at the membrane interface New research by the Bublitz group in collaboration with the Danish drug discovery company PCovery, describes a new class of compounds that inhibit the growth of fungal cells by disrupting their plasma membrane potential Published: 9 January 2018
Prof Tony Watts swaps the lab bench for the back bench
Prof Tony Watts Tony Watts has been paired with Ms Layla Moran, the Liberal Democrat MP for Oxford West and Abindgon, for the 17th Royal Society scientists' pairing scheme. This innovative scheme pairs scientists with parliamentarians and civil servants. Published: 21 December 2017
Kim Nasmyth 2018 Breakthrough Prize in Life Sciences
Alt Text Our congratulations to Kim Nasmyth on the award of the 2018 Breakthrough Prize ('The Oscars of Science') in Life Sciences. See also: https://breakthroughprize.org/News/41 Published: 4 December 2017
Oxford iGEM team wins Gold medal and Award for Best Diagnostics Project
iGem Logo The 2017 Oxford University iGEM team have just returned from the competition in Boston with not only a Gold medal but also the extremely competitive award for Best Diagnostics Project in the undergraduate category Published: 16 November 2017

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Welcome

Mark Sansom, Head of Department

The Department of Biochemistry at the University of Oxford is a centre for world class research and teaching of all aspects of Biochemistry by staff from many different backgrounds and nationalities. Our research addresses a wide range of questions relating to the fundamental basis of all cellular life from man to microbes. This work explains the structures and functions of proteins and nucleic acids, and in doing so addresses the mechanisms of many human diseases. Using this knowledge, other researchers aim to create new vaccines, antiviral and antibacterial therapies to protect and treat humans across the world.

You can read more about the details of our current work and other aspects of the department, including undergraduate teaching and public outreach activities, on these web pages.

Professor Mark Sansom, Head of Department

News Highlight

Key step in cellular glycosylation revealed in new crystal structure of a Golgi nucleotide sugar transporter

New research by the Newstead group, published in Nature, reveals the first crystal structure for a member of the nucleotide sugar transporter (NST) superfamily and provides fundamental new insights into how glycosylation is regulated in the cell.

In eukaryotes, glycosylation occurs in the lumen of the endoplasmic reticulum and the Golgi apparatus. Nucleotide sugars required for glycosylation are imported into the lumen of these organelles by a family of intracellular NSTs. But how NSTs recognize and transport nucleotide sugars has been unclear.

Figure. A. Nucleotide sugar transporters function to shuttle activated sugar donors (sugar-NDP) across the endoplasmic reticulum (ER) and Golgi membranes. NDP, nucleoside diphosphate; NMP, nucleoside monophosphate. B, Crystal structure of Vrg4 viewed from the Golgi membrane.

Figure. A. Nucleotide sugar transporters function to shuttle activated sugar donors (sugar-NDP) across the endoplasmic reticulum (ER) and Golgi membranes. NDP, nucleoside diphosphate; NMP, nucleoside monophosphate. B, Crystal structure of Vrg4 viewed from the Golgi membrane (Click to Enlarge)

Now, work from the Newstead lab, has revealed the crystal structure of the yeast GDP-mannose transporter, Vrg4. The structure shows how the monosaccharide, GDP-mannose is recognised by the transporter and identifies new sequence motifs responsible for selecting different types of nucleotide sugar molecules in the cell. Intriguingly, the work also reveals that Vrg4 will only function in the presence of short chain lipid molecules, providing the first experimental evidence that membrane bilayer thickness may regulate intracellular transport in the secretory pathway.

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Seminars

Departmental Seminar Dr Naoko Mizuno, 'Cell shape formation controlled by cytoskeleton' Friday 23rd Feb, 11:00 main seminar room, New Biochemistry Building
SBMB Seminar Series Naoko Mizuno, 'Title TBC' Friday 23rd Feb, 11:00 Main Seminar Roon, New Biochemistry Building
Special Seminar Professor Benoit Kornmann, 'Organelle contact sites: what are they, what are they good for, and how can they be bad' Tuesday 27th Feb, 9:00 Main Seminar Room, New Biochemistry Building
Special Seminar Dr. Juanma Vaquerizas, '3D Chromatin Conformation during early Embryonic Development' Tuesday 27th Feb, 9:35 Main Seminar Room, New Biochemistry Building


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Athena Swan Silver Award