Sir John Walker
John Ernest Walker
7 January 1941
|Education||Rastrick Grammar School|
|Alma mater||University of Oxford (BA, DPhil)|
Christina Westcott(m. 1963)
|Institutions|| University of Oxford |
Laboratory of Molecular Biology
University of Cambridge
|Thesis||Studies on naturally occurring peptides (1970)|
|Doctoral advisor||Edward Abraham|
Sir John Ernest WalkerAs of 2015 [update] Walker is Emeritus Director and Professor at the MRC Mitochondrial Biology Unit in Cambridge, and a Fellow of Sidney Sussex College, Cambridge.(born 7 January 1941) is a British chemist who won the Nobel Prize in Chemistry in 1997.
Walker was born in Halifax, Yorkshire, the son of Thomas Ernest Walker, a stonemason, and Elsie Lawton, an amateur musician. He was brought up with his two younger sisters (Judith and Gen) in a rural environment and went to Rastrick Grammar School. At school, he was a keen sportsman and specialized in physical sciences and mathematics during his final three years there. He received a Bachelor of Arts degree in Chemistry from St Catherine's College, Oxford.Walker began his study of peptide antibiotics with Edward Abraham at Oxford in 1965 and received his Doctor of Philosophy degree in 1969. During this period, he became interested in developments in molecular biology.
From 1969 to 1971, Walker worked at the University of Wisconsin–Madison, and from 1971–1974 in France. He met Fred Sanger in 1974 at a workshop at the University of Cambridge. This resulted in an invitation to work at the Laboratory of Molecular Biology of the Medical Research Council, which became a long-term appointment. Among the other staff was Francis Crick, who was well known for his discovery of the molecular structure of DNA. At first, he analyzed the sequences of proteins and then uncovered details of the modified genetic code in mitochondria. In 1978, he decided to apply protein chemical methods to membrane proteins. In this way, Walker characterized the subunit composition of proteins in the mitochondrial membrane and the DNA sequence of the mitochondrial genome.
His landmark crystallographic studies of the F1-ATPase, the catalytic region of the ATP synthase (done in collaboration with crystallographer Andrew Leslie), from bovine heart mitochondria revealed the three catalytic sites in three different conformations imposed by the position of the asymmetric central stalk. This structure supported the binding change mechanism and rotary catalysis for the ATP synthase (and related enzymes), one of the catalytic mechanisms proposed by Paul Boyer. This work, published in 1994, led to Walker's share of the 1997 Nobel prize for chemistry. Since this structure, Walker and his colleagues have produced most of the crystal structures in the PDB of mitochondrial ATP synthase, including transition state structures and protein with bound inhibitors and antibiotics. Scientists trained in Walker's group at the MRC Laboratory of Molecular Biology in Cambridge or MRC Mitochondrial Biology Unit have gone on to determine crystal bacterial complex I and cryo-EM maps of mitochondrial complex I and vacuolar type ATPases.
Students and postdoctoral research fellows who studied with John Walker who have gone on to independent research careers include:
Walker was elected an EMBO Member in 1984.He shared his Nobel Prize with the American chemist Paul D. Boyer for their elucidation of the enzymatic mechanism underlying the synthesis of adenosine triphosphate. They also shared the prize with Danish chemist Jens C. Skou for research unrelated to theirs (Discovery of the Na+/K+-ATPase). Sir John was knighted in 1999 for services to molecular biology. He is a member of the Advisory Council for the Campaign for Science and Engineering. He was elected a Fellow of the Royal Society (FRS) in 1995. Walker is also a Foreign Associate of the National Academy of Sciences and an Honorary Fellow of St Catherine's College, Oxford. He became a foreign member of the Royal Netherlands Academy of Arts and Sciences in 1999. In 2012 he was awarded the Copley Medal.
Walker married Christina Westcott in 1963, and has two daughters.
Max Ferdinand Perutz was an Austrian-born British molecular biologist, who shared the 1962 Nobel Prize for Chemistry with John Kendrew, for their studies of the structures of haemoglobin and myoglobin. He went on to win the Royal Medal of the Royal Society in 1971 and the Copley Medal in 1979. At Cambridge he founded and chaired (1962–79) The Medical Research Council (MRC) Laboratory of Molecular Biology (LMB), fourteen of whose scientists have won Nobel Prizes. Perutz's contributions to molecular biology in Cambridge are documented in The History of the University of Cambridge: Volume 4 published by the Cambridge University Press in 1992.
ATP synthase is an enzyme that creates the energy storage molecule adenosine triphosphate (ATP), forming it from adenosine diphosphate (ADP) and inorganic phosphate (Pi). The overall reaction catalyzed by ATP synthase is:
Sir John Cowdery Kendrew, was an English biochemist, crystallographer, and science administrator. Kendrew shared the 1962 Nobel Prize in Chemistry with Max Perutz, for their work at the Cavendish Laboratory to investigate the structure of heme-containing proteins.
Sir Gregory Paul Winter is a Nobel Prize-winning British biochemist best known for his work on the therapeutic use of monoclonal antibodies. His research career has been based almost entirely at the MRC Laboratory of Molecular Biology and the MRC Centre for Protein Engineering, in Cambridge, England.
Michael Levitt, is an American-British-Israeli-South African biophysicist and a professor of structural biology at Stanford University, a position he has held since 1987. Levitt received the 2013 Nobel Prize in Chemistry, together with Martin Karplus and Arieh Warshel, for "the development of multiscale models for complex chemical systems".
The Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) is a research institute in Cambridge, England, involved in the revolution in molecular biology which occurred in the 1950–60s. Since then it has remained a major medical research laboratory with a much broader focus.
Richard Henderson is a Scottish molecular biologist and biophysicist and pioneer in the field of electron microscopy of biological molecules. Henderson shared the Nobel Prize in Chemistry in 2017 with Jacques Dubochet and Joachim Frank.
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The MRC Mitochondrial Biology Unit is a department of the School of Clinical Medicine at the University of Cambridge, funded through a strategic partnership between the Medical Research Council and the University. It is located at the Addenbrooke’s Hospital / Cambridge Biomedical Campus site in Cambridge, England. The unit is concerned with the study of the mitochondrion, as this organelle has a varied and critical role in many aspects of eukaryotic metabolism and is implicated in many metabolic, degenerative, and age-related human diseases.
MT-ATP8 is a mitochondrial gene with the full name 'mitochondrially encoded ATP synthase membrane subunit 8' that encodes a subunit of mitochondrial ATP synthase, ATP synthase Fo subunit 8. This subunit belongs to the Fo complex of the large, transmembrane F-type ATP synthase. This enzyme, which is also known as complex V, is responsible for the final step of oxidative phosphorylation in the electron transport chain. Specifically, one segment of ATP synthase allows positively charged ions, called protons, to flow across a specialized membrane inside mitochondria. Another segment of the enzyme uses the energy created by this proton flow to convert a molecule called adenosine diphosphate (ADP) to ATP. Subunit 8 differs in sequence between Metazoa, plants and Fungi.
ATP synthase F1 subunit alpha, mitochondrial is an enzyme that in humans is encoded by the ATP5F1A gene.
ATP synthase subunit delta, mitochondrial, also known as ATP synthase F1 subunit delta or F-ATPase delta subunit is an enzyme that in humans is encoded by the ATP5F1D gene. This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation.
ATP synthase F1 subunit epsilon, mitochondrial is an enzyme that in humans is encoded by the ATP5F1E gene. The protein encoded by ATP5F1E is a subunit of ATP synthase, also known as Complex V. Variations of this gene have been associated with mitochondrial complex V deficiency, nuclear 3 (MC5DN3) and Papillary Thyroid Cancer.
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The Walker A and Walker B motifs are protein sequence motifs, known to have highly conserved three-dimensional structures. These were first reported in ATP-binding proteins by Walker and co-workers in 1982.
Laurence Harris Pearl FRS FMedSci is a British biochemist and structural biologist who is currently Professor of Structural Biology in the Genome Damage and Stability Centre and was Head of the School of Life Sciences at the University of Sussex.
Dario Alessi FRSE FRS is a biochemist, Director of the Medical Research Council Protein Phosphorylation and Ubiquitylation Unit and Professor of Signal Transduction, at the School of Life Sciences, University of Dundee.
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Leonid A. Sazanov is a Professor at the Institute of Science and Technology Austria (IST). Sazanov research explores the structure and function of large membrane protein complexes from the domain of bioenergetics. These molecular machines interconvert redox energy and proton motive force across biological membranes using a variety of mechanisms.
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