Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Larry H. Weaver"'
Publikováno v:
Journal of Molecular Biology. 357:509-523
BirA catalyzes the adenylation and subsequent covalent attachment of biotin to the biotin carboxyl carrier protein (BCCP). In the absence of apo-BCCP, biotin-5'-AMP acts as a co-repressor that induces BirA dimerization and binding to the bio operator
Autor:
Brian W. Matthews, Blaine H. M. Mooers, Nadine C. Gassner, Michael L. Quillin, Robert D. Busam, Walter A. Baase, Joel D. Lindstrom, Larry H. Weaver
Publikováno v:
Biophysical Chemistry. 100:325-340
In order to further explore the tolerance of proteins to amino acid substitutions within the interior, a series of core residues was replaced by methionine within the C-terminal domain of T4 lysozyme. By replacing leucine, isoleucine, valine and phen
Autor:
Brian W. Matthews, Joel D. Lindstrom, Walter A. Baase, Larry H. Weaver, Anthony R. Poteete, Jonathan W. Wray
Publikováno v:
Journal of Molecular Biology. 292:1111-1120
The mutation Glu108 → Val (E108V) in T4 lysozyme was previously isolated as a second-site revertant that specifically compensated for the loss of function associated with the destabilizing substitution Leu99 → Gly (L99G). Surprisingly, the two si
Publikováno v:
Journal of Structural Biology. 117:165-172
Certain peptides with sequences related to part of the major histocompatibility complex class I antigen enhance the action of insulin. These peptides also aggregate into fibrous structures that seem to be related to their biological activity. In the
Publikováno v:
Nature Structural & Molecular Biology. 2:1007-1011
Here we show that the substitution Thr 26--His in the active site of T4 lysozyme causes the product to change from the alpha- to the beta-anomer. This implies an alteration in the catalytic mechanism of the enzyme. From the change in product, togethe
Publikováno v:
Journal of Molecular Biology. 245:54-68
The structure of goose egg-white lysozyme (GEWL) has been refined to an R-value of 15.9% at 1.6 A resolution. Details of the structure determination, the refinement and the structure itself are presented. The structure of a complex of the enzyme with
Publikováno v:
Journal of molecular biology. 337(5)
Sampling receptor flexibility is challenging for database docking. We consider a method that treats multiple flexible regions of the binding site independently, recombining them to generate different discrete conformations. This algorithm scales line
Publikováno v:
Journal of molecular biology. 322(2)
Prediction of interaction energies between ligands and their receptors remains a major challenge for structure-based inhibitor discovery. Much effort has been devoted to developing scoring schemes that can successfully rank the affinities of a divers
Publikováno v:
Protein science : a publication of the Protein Society. 10(12)
A model is suggested for the complex between the biotin repressor of Escherichia coli, BirA, and BCCP, the biotin carboxyl carrier protein to which BirA transfers biotin. The model is consistent with prior physical and biochemical studies. Measuremen
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 98(11)
The Escherichia coli biotin repressor binds to the biotin operator to repress transcription of the biotin biosynthetic operon. In this work, a structure determined by x-ray crystallography of a complex of the repressor bound to biotin, which also fun