Andrew Carter became interested in structural biology as an undergraduate at the University of Oxford. This led him to start a PhD in 1999 with Venki Ramakrishnan at the MRC Laboratory of Molecular Biology in Cambridge. He worked as part of the team that determined the X-ray crystal structure of the small (30S) ribosomal subunit. In addition he solved structures of the ribosome bound to antibiotics and the protein initiation factor IF1. After his PhD he spent an extra year in Cambridge as a junior research fellow at Clare College, before moving in 2003 to Ron Vale’s lab at the University of California San Francisco where he started working on the microtubule motor protein dynein. In 2008 he accepted a group leader position back at the MRC-LMB but put it on hold in order to focus on crystallizing the main 300kD dynein's motor domain. In 2010 he returned to Cambridge to set up his own lab.
Structure of the dynein motor domain
Dyneins are motor proteins that power the beating of cilia and flagella, transport a large variety of intracellular cargos and play important roles in mitosis. Prof. Carter will discuss new crystal structures of the ring-shaped S.cerevisiae cytoplasmic dynein motor domain in different nucleotide states at 3.3 Å – 3.6 Å which provide novel insights into how the energy of ATP hydrolysis is used to produce movement. In all these structures the linker domain, the motile element which arches over the ring and moves in response to ATP-hydrolysis, is firmly attached to ring. Carter lab uses mutagenesis and in vitro motility assays to verify the relevance of this state and combine their findings into a mechanistic model of the dynein motor domain.
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