Corepressor-induced organization and assembly of the biotin repressor: A model for allosteric activation of a transcriptional regulator - Test2 - elhamkhani - TriplyDB

Corepressor-induced organization and assembly of the biotin repressor: A model for allosteric activation of a transcriptional regulator

Corepressor-induced organization and assembly of the biotin repressor: A model for allosteric activation of a transcriptional regulator

http://www.wikidata.org/entity/Q27631783

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The N-terminal domain of human holocarboxylase synthetase facilitates biotinylation via direct interaction with the substrate protein N- and C-terminal domains in human holocarboxylase synthetase participate in substrate recognition Protein biotinylation visualized by a complex structure of biotin protein ligase with a substrate A protein functional leap: how a single mutation reverses the function of the transcription regulator TetR Active site conformational changes upon reaction intermediate biotinyl-5'-AMP binding in biotin protein ligase fromMycobacterium tuberculosis Vhr1p, a new transcription factor from budding yeast, regulates biotin-dependent expression of VHT1 and BIO5.Meet the neighbors: Mapping local protein interactomes by proximity-dependent labeling with BioID Detection of trans-cis flips and peptide-plane flips in protein structures The C-terminal domain of biotin protein ligase from E. coli is required for catalytic activity Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor The Mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine dyad acyltransferase Brucella BioR regulator defines a complex regulatory mechanism for bacterial biotin metabolism Selection of an active enzyme by phage display on the basis of the enzyme's catalytic activity in vivo.Ligand specificity of group I biotin protein ligase of Mycobacterium tuberculosis Allosteric signaling in the biotin repressor occurs via local folding coupled to global dampening of protein dynamics.Regulating transcription regulators via allostery and flexibility Common peptides study of aminoacyl-tRNA synthetases Disordered to ordered folding in the regulation of diphtheria toxin repressor activity.Biotin and Lipoic Acid: Synthesis, Attachment, and Regulation.Directed evolution of the substrate specificity of biotin ligase.Successful conversion of the Bacillus subtilis BirA Group II biotin protein ligase into a Group I ligase Profligate biotin synthesis in α-proteobacteria - a developing or degenerating regulatory system?Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus.Deciphering a unique biotin scavenging pathway with redundant genes in the probiotic bacterium Lactococcus lactis Functional definition of BirA suggests a biotin utilization pathway in the zoonotic pathogen Streptococcus suis Allostery: absence of a change in shape does not imply that allostery is not at play.Extrinsic interactions dominate helical propensity in coupled binding and folding of the lactose repressor protein hinge helix.The wing of a winged helix-turn-helix transcription factor organizes the active site of BirA, a bifunctional repressor/ligase.Protein:protein interactions in control of a transcriptional switch.Marked by association: techniques for proximity-dependent labeling of proteins in eukaryotic cells.Binding specificity and the ligand dissociation process in the E. coli biotin holoenzyme synthetase.Proximity labeling of interacting proteins: Application of BioID as a discovery tool.Structural characterization of Staphylococcus aureus biotin protein ligase and interaction partners: an antibiotic target The specialized secretory apparatus ESX-1 is essential for DNA transfer in Mycobacterium smegmatis.Promiscuous protein biotinylation by Escherichia coli biotin protein ligase.Thermodynamic and structural investigation of bispecificity in protein-protein interactions.Sequence-function relationships in folding upon binding.Imaging activity-dependent regulation of neurexin-neuroligin interactions using trans-synaptic enzymatic biotinylation.Biochemical properties and biological function of a monofunctional microbial biotin protein ligase Biotin sensing at the molecular level.

P2860

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P2860

Corepressor-induced organization and assembly of the biotin repressor: A model for allosteric activation of a transcriptional regulator

http://www.wikidata.org/entity/Q27631783

description

2001 nî lūn-bûn

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2001年の論文

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Corepressor-induced organizati ...... of a transcriptional regulator

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Corepressor-induced organizati ...... of a transcriptional regulator

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Proceedings of the National Academy of Sciences of the United States of America

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Corepressor-induced organizati ...... of a transcriptional regulator

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B W Matthews

http://www.w3.org/2001/XMLSchema#string

D Beckett

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K Kwon

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L H Weaver

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P2860

Structures of the apo- and the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriae

Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

A closer view of the conformation of the Lac repressor bound to operator

Structural basis of gene regulation by the tetracycline inducible Tet repressor-operator system

Mechanism of corepressor-mediated specific DNA binding by the purine repressor

Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by alpha helices

Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coli

Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex

Crystal structure of a complex of Escherichia coli glycerol kinase and an allosteric effector fructose 1,6-bisphosphate

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10.1073/PNAS.111128198

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