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
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Outstanding departmental research recognised in REF 2014
Image: Jeremy Rowntree The Department of Biochemistry has contributed to the largest volume of world-leading and internationally excellent research in the REF 2014 exercise, as announced today. Published: 18 December 2014
Balancing diversity with conservation - learning tricks from malaria parasite proteins
The structure of a complex of the CIDR domain of a PfEMP1 variant (yellow) bound to EPCR (blue). A phenylalanine of the CIDR domain, at the centre of the interface, is shown as pink sticks A new study sheds light on how the malaria parasite can evade the bodys defences whilst retaining the ability to interact with and thrive in its host Published: 9 December 2014
Department marks 50+5 anniversary
Peter Holmes, Linda Partridge, Mark Sansom, Jane Mellor, Matt Higgins, Gerard Evan, Kim Nasmyth and Alan Fersht at the 50+5 event The Department has celebrated 5 years of occupancy of the New Biochemistry Building alongside the 50th anniversary of the Oxford University Biochemical Society (OUBS) Published: 4 December 2014

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Athena Swan Bronze Award

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Welcome

The Department of Biochemistry

Welcome to the Department of Biochemistry, part of the University of Oxford's Medical Sciences Division. We are one of the largest Biochemistry departments in the world and carry out world-class research and teaching. Our researchers come from a range of disciplines and work in a collaborative environment on all aspects of modern molecular and cellular biochemistry. We hope you enjoy reading more about our activities on these pages.

Professor Mark Sansom, Head of Department

News Highlight

Closing the cohesin ring round sister chromatids

Crystal structure of the Smc3 head with coiled coil section (Smc3hdCC) in complex with the N-terminal domain of kleisin (Scc1-N). The Smc1 head domain (Smc1hd) is shown in red in dimer formation with the Smc3 head

Crystal structure of the Smc3 head with coiled coil section (Smc3hdCC) in complex with the N-terminal domain of kleisin (Scc1-N). The Smc1 head domain (Smc1hd) is shown in red in dimer formation with the Smc3 head (Click to enlarge)

A new study completes the structural and functional picture of the cohesin ring that traps DNA during mitosis until the critical moment of cell division.

The researchers behind the work, from Kim Nasmyth's lab in the department and the lab of Jan Löwe at the MRC LMB in Cambridge, describe their findings in a recent paper in Science (1).

Using the new structural information, the group has confirmed the presence of the tripartite cohesin ring in living cells and can begin to look at the mechanisms behind cohesin's functions.

Cohesin is a highly conserved complex comprised of subunits Smc1 and Smc3 forming a v-shaped conformation. These associate with a kleisin subunit to form what is believed to be a ring that holds sister chromatids together during mitosis until exactly the right time for their separation (2).

The interface between Smc3 and kleisin is a key regulatory one. Smc3 acetylation ensures that the ring is locked tightly shut, but release can be triggered by regulatory subunits that allow exit of the sister DNAs.

As Thomas Gligoris, one of the postdocs in the Nasmyth lab, explains, an understanding of this interface has so far eluded researchers. 'We had the crystal structure of the Smc1/Smc3 interface and also the Smc1/kleisin interface but were missing the structure of the Smc3/kleisin interface.'

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Seminars

Departmental Seminar Rudy Behnia, 'Processing Properties of ON and OFF Pathways for Drosophila Motion Detection' Monday 5th Jan, 12:00 , The Oxford Martin School Old Indian Institute, 34 Broad Street, Oxford,
Special Seminar Dr. Alan Brown, ''High-resolution cryo-EM; revealing the mysteries of the mitochondrial ribosome'' Friday 16th Jan, 10:00 Main Meeting Room, New Biochemistry Building
Biochemistry Department Seminar Professor Dr. Andreas Plueckthun, 'Evolving GPCRs to high stability: enabling structural biology and drug screening' Monday 26th Jan, 12:00 Main Meeting Room, New Biochemistry Building
2nd Louise Johnson Memorial Lecture Professor John Kuriyan, 'tbc' Tuesday 19th May, 16:00 Main Meeting Room, New Biochemistry Building


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