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Bacillus thuringiensis CryIA(a) insecticidal toxin: crystal structure and channel formation.
Comparison with the structure of CryIIIA, a coleopteran-specific toxin, shows that although the fold of these two proteins is similar, there are significant structural differences within domain II, which supports the conclusions from genetic studies that domain II is involved in recognition and binding to cell surface receptors.
The a/ hydrolase fold
Method and apparatus for performing 2-bit, non-restore, look-ahead, binary division for a digital processor wherein 2 quotient bits are generated simultaneously during one adder cycle, the cycle length being essentially limited to the time needed by the adder to perform subtraction.
The Architecture of the Multisubunit TRAPP I Complex Suggests a Model for Vesicle Tethering
Structural Basis for Fe–S Cluster Assembly and tRNA Thiolation Mediated by IscS Protein–Protein Interactions
Crystal structures reveal how distinct sites on the cysteine desulfurase IscS bind two different sulfur-acceptor proteins, IscU and TusA, to transfer sulfur atoms for iron-sulfur cluster biosynthesis…
The Structure of calnexin, an ER chaperone involved in quality control of protein folding.
Crystal structure of the bb' domains of the protein disulfide isomerase ERp57.
Structure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex
- M. Boniecki, S. Freibert, U. Mühlenhoff, R. Lill, M. Cygler
- ChemistryNature Communications
- 3 November 2017
Crystal structures of three different NFS1-ISD11-ACP complexes with and without ISCU are presented, and SAXS analyses are used to define the 3D architecture of the complete mitochondrial Fe/S cluster biosynthetic complex.
The alpha/beta hydrolase fold.
There are now four groups of enzymes which contain catalytic triads and which are related by convergent evolution towards a stable, useful active site: the eukaryotic serine proteases, the cysteine protease, subtilisins and the alpha/beta hydrolase fold enzymes.
Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment.
- R. Coulombe, P. Grochulski, J. Sivaraman, R. Ménard, J. Mort, M. Cygler
- Biology, ChemistryThe EMBO journal
- 1 October 1996
The fold of the prosegment and the mechanism by which it inhibits the enzymatic activity of procathepsin L is similar to that observed in procat hepsin B despite differences in length and sequence, suggesting that this mode of inhibition is common to all enzymes from the papain superfamily.
Antibodies to DNA
- W. Anderson, M. Cygler, R. Braun, Jeremy S. Lee
- BiologyBioEssays : news and reviews in molecular…
- 1 February 1988
Antibodies that are specific for DNA provide an excellent system for studying the protein‐nucleic acid interactions that allow proteins to recognize specific DNA structures or sequences.