A5073944951- Enzyme Structure and Function
- Protein Structure and Dynamics
- Heat shock proteins research
- Toxin Mechanisms and Immunotoxins
- RNA and protein synthesis mechanisms
- Microbial Natural Products and Biosynthesis
- Biochemical and Structural Characterization
- Bacterial Genetics and Biotechnology
- Enzyme Catalysis and Immobilization
- Microbial Metabolic Engineering and Bioproduction
- Ubiquitin and proteasome pathways
- Neurological diseases and metabolism
- Enzyme Production and Characterization
- Genomics and Phylogenetic Studies
- Viral Infectious Diseases and Gene Expression in Insects
- 14-3-3 protein interactions
- thermodynamics and calorimetric analyses
- Prion Diseases and Protein Misfolding
- Advanced Proteomics Techniques and Applications
- Endoplasmic Reticulum Stress and Disease
- Antimicrobial Peptides and Activities
- Biochemical and Molecular Research
- Parasite Biology and Host Interactions
- Peptidase Inhibition and Analysis
- Advanced Glycation End Products research
University of Bristol
2005-2024
University of British Columbia
2005
University of Southampton
2005
Howard Hughes Medical Institute
1996-1998
Yale University
1998
Pediatrics and Genetics
1997
University of Sheffield
1996
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTBinding and hydrolysis of nucleotides in the chaperonin catalytic cycle: Implications for mechanism assisted protein foldingGraham S. Jackson, Rosemary A. Staniforth, David J. Halsall, Tony Atkinson, John Holbrook, Anthony R. Clarke, Steven G. BurstonCite this: Biochemistry 1993, 32, 10, 2554–2563Publication Date (Print):March 16, 1993Publication History Published online1 May 2002Published inissue 16 March...
The refolding of lactate dehydrogenase fully unfolded in 4 M guanidinium chloride was initiated by dilution into assay buffer, and the emergence active enzyme recorded. This performed presence following chaperonin complexes medium: chaperonin-60 (cpn60), cpn60-MgATP, cpn60-Mgp[NH]ppA, cpn60-MgADP both absence chaperonin-10 (cpn10). For each nucleotide-chaperonin complex studied, effect nucleotide concentration measured. Dissociation constants (Kd) for LDH bound to various were derived...
Mitochondrial malate dehydrogenase (mMDH) folds more rapidly in the presence of GroEL, GroES and ATP than it does unassisted. The increase folding rate as a function concentration GroEL-ES reaches maximum at stoichiometry which is approximately equimolar (mMDH subunits:GroEL oligomer) with an apparent dissociation constant K' for GroE acceptor state least 1 x 10(-8) M. However, even chaperonin concentrations are 4000 K', i.e. negligible free mMDH, observed substrate remains its optimum,...
mMDH and cMDH are structurally homologous enzymes which show very different responses to chaperonins during folding. The hydrophilic stable is bound by cpn60 but released MG‐ATP alone, while the hydrophobic unstable requires both Mg‐ATP cpn 10. Citrate equalises stability of native state two proteins has no effect on co‐chaperonin requirement, implying that hydrophobicity, not stability, determining factor. yield rate folding unaffected markedly increased presence cpn60, cpn10 Mg‐ATP. In 200...
The actinorhodin (act) synthase acyl carrier protein (ACP) from Streptomyces coelicolor plays a central role in polyketide biosynthesis. Polyketide intermediates are bound to the free sulfhydryl group of phosphopantetheine arm that is covalently linked conserved serine residue holo form ACP. solution NMR structures both apo and forms ACP reported, which represents first high resolution comparison these two an Ensembles twenty were calculated yielded atomic root mean square deviations...
Significance Small-molecule inhibitors of enzymes are commonly derived from native ligands and represent invaluable extensively applied tools in chemical biology. In addition to the well-known issue selectivity, paradoxical curiosities were described over decades that have wide implications drug discovery treatment. Of particular interest observations where low concentrations may activate their targets instead causing partial inhibition. Our conceptual analysis explains general phenomenon...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTThe energetics and cooperativity of protein folding: a simple experimental analysis based upon the solvation internal residuesRosemary A. Staniforth, Steven G. Burston, Corinne J. Smith, Graham S. Jackson, Ian Badcoe, Tony Atkinson, John Holbrook, Anthony R. ClarkeCite this: Biochemistry 1993, 32, 15, 3842–3851Publication Date (Print):April 20, 1993Publication History Published online1 May 2002Published inissue 20 April...
The protein Sup35 has prion properties. Its aggregation is at the origin of [PSI(+)] trait in Saccharomyces cerevisiae. In vitro, N-terminal domain Sup35p alone or with middle assembles into fibrils that exhibit characteristics amyloids. vast majority vitro studies on assembly have been performed using Sup35pNM, as made Sup35pNM assembled propagate when reintroduced yeast cells. Little known about full-length and role functional C-terminal protein. Here we report a systematic comparison...
During polyketide biosynthesis, malonyl groups are transferred to the acyl carrier protein (ACP) component of synthase (PKS), and it has been shown that a number type II ACPs undergo rapid self-acylation from malonyl-CoA in absence malonyl-CoA:holo-acyl transacylase (MCAT). More recently, however, observation self-malonylation ascribed contamination with Escherichia coli MCAT (FabD) rather than an intrinsic property ACP. The wild-type apo-ACP actinorhodin (act) PKS Streptomyces coelicolor...
Malonylation of an acyl carrier protein (ACP) by malonyl Coenzyme A-ACP transacylase (MCAT) is fundamental to bacterial fatty acid biosynthesis. Here, we report the structure Steptomyces coelicolor (Sc) synthase (FAS) ACP and studies its binding MCAT. The adopts α-helical bundle common other known proteins. Sc FAS shows close structural homology with ACPs less similarity actinorhodin (act) polyketide (PKS) where orientation helix I differs. NMR experiments were used map This data suggests...
A molecular description of the complete reaction cycle bona fide natural Diels–Alderase AbyU is presented, revealing mechanistic intricacies this enzyme system.
Bacillus stearothermophilus phosphoglycerate kinase (bsPGK) is a monomeric enzyme of 394 residues comprising two globular domains (N and C), covalently linked by an interdomain α-helix (residues 170−185). The molecule folds to the native state in three stages. In first, each domain rapidly independently collapses form intermediate which N-domain stabilized 5.1 kcal mol-1 C-domain 3.3 over their respective unfolded conformations. then converts folded at rate 1.2 s-1 (ΔGI-F = 3.8 mol-1),...