Substrate Channel Flexibility in Pseudomonas aeruginosa MurB Accommodates Two Distinct Substrates

10.1371/journal.pone.0066936

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Main Authors:	Chen M.W., Lohkamp B., Schnell R., Lescar J., Schneider G.
Other Authors:	DUKE-NUS MEDICAL SCHOOL
Format:	Article
Published:	Public Library of Science 2020
Subjects:	bacterial enzyme flavine adenine nucleotide nicotinamide nicotinamide adenine dinucleotide phosphate potassium ion unclassified drug uridine diphosphate n acetylglucosamine enolpyruvate reductase bacterial protein oxidoreductase potassium recombinant protein UDP-N-acetylglucosamine-enolpyruvate uridine diphosphate n acetylglucosamine article binding site complex formation controlled study crystal structure enzyme kinetics enzyme localization enzyme substrate Escherichia coli nonhuman nucleotide sequence protein conformation protein structure Pseudomonas aeruginosa species comparison amino acid sequence analogs and derivatives biosynthesis chemistry enzyme active site enzyme specificity enzymology genetics isolation and purification metabolism molecular dynamics sequence alignment X ray crystallography Bacteria (microorganisms) Amino Acid Sequence Bacterial Proteins Binding Sites Catalytic Domain Crystallography, X-Ray Flavin-Adenine Dinucleotide Molecular Dynamics Simulation NADP Oxidoreductases Potassium Recombinant Proteins Sequence Alignment Substrate Specificity Uridine Diphosphate N-Acetylglucosamine
Online Access:	https://scholarbank.nus.edu.sg/handle/10635/166195
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Institution:	National University of Singapore

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spelling	sg-nus-scholar.10635-1661952023-10-31T08:46:12Z Substrate Channel Flexibility in Pseudomonas aeruginosa MurB Accommodates Two Distinct Substrates Chen M.W. Lohkamp B. Schnell R. Lescar J. Schneider G. DUKE-NUS MEDICAL SCHOOL bacterial enzyme flavine adenine nucleotide nicotinamide nicotinamide adenine dinucleotide phosphate potassium ion unclassified drug uridine diphosphate n acetylglucosamine enolpyruvate reductase bacterial protein flavine adenine nucleotide nicotinamide adenine dinucleotide phosphate oxidoreductase potassium recombinant protein UDP-N-acetylglucosamine-enolpyruvate uridine diphosphate n acetylglucosamine article binding site complex formation controlled study crystal structure enzyme kinetics enzyme localization enzyme substrate Escherichia coli nonhuman nucleotide sequence protein conformation protein structure Pseudomonas aeruginosa species comparison amino acid sequence analogs and derivatives biosynthesis chemistry enzyme active site enzyme specificity enzymology genetics isolation and purification metabolism molecular dynamics Pseudomonas aeruginosa sequence alignment X ray crystallography Bacteria (microorganisms) Escherichia coli Pseudomonas aeruginosa Amino Acid Sequence Bacterial Proteins Binding Sites Catalytic Domain Crystallography, X-Ray Escherichia coli Flavin-Adenine Dinucleotide Molecular Dynamics Simulation NADP Oxidoreductases Potassium Pseudomonas aeruginosa Recombinant Proteins Sequence Alignment Substrate Specificity Uridine Diphosphate N-Acetylglucosamine 10.1371/journal.pone.0066936 PLoS ONE 8 6 e66936 2020-03-31T03:01:41Z 2020-03-31T03:01:41Z 2013 Article Chen M.W., Lohkamp B., Schnell R., Lescar J., Schneider G. (2013). Substrate Channel Flexibility in Pseudomonas aeruginosa MurB Accommodates Two Distinct Substrates. PLoS ONE 8 (6) : e66936. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0066936 19326203 https://scholarbank.nus.edu.sg/handle/10635/166195 Public Library of Science Unpaywall 20200320
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	bacterial enzyme flavine adenine nucleotide nicotinamide nicotinamide adenine dinucleotide phosphate potassium ion unclassified drug uridine diphosphate n acetylglucosamine enolpyruvate reductase bacterial protein flavine adenine nucleotide nicotinamide adenine dinucleotide phosphate oxidoreductase potassium recombinant protein UDP-N-acetylglucosamine-enolpyruvate uridine diphosphate n acetylglucosamine article binding site complex formation controlled study crystal structure enzyme kinetics enzyme localization enzyme substrate Escherichia coli nonhuman nucleotide sequence protein conformation protein structure Pseudomonas aeruginosa species comparison amino acid sequence analogs and derivatives biosynthesis chemistry enzyme active site enzyme specificity enzymology genetics isolation and purification metabolism molecular dynamics Pseudomonas aeruginosa sequence alignment X ray crystallography Bacteria (microorganisms) Escherichia coli Pseudomonas aeruginosa Amino Acid Sequence Bacterial Proteins Binding Sites Catalytic Domain Crystallography, X-Ray Escherichia coli Flavin-Adenine Dinucleotide Molecular Dynamics Simulation NADP Oxidoreductases Potassium Pseudomonas aeruginosa Recombinant Proteins Sequence Alignment Substrate Specificity Uridine Diphosphate N-Acetylglucosamine
spellingShingle	bacterial enzyme flavine adenine nucleotide nicotinamide nicotinamide adenine dinucleotide phosphate potassium ion unclassified drug uridine diphosphate n acetylglucosamine enolpyruvate reductase bacterial protein flavine adenine nucleotide nicotinamide adenine dinucleotide phosphate oxidoreductase potassium recombinant protein UDP-N-acetylglucosamine-enolpyruvate uridine diphosphate n acetylglucosamine article binding site complex formation controlled study crystal structure enzyme kinetics enzyme localization enzyme substrate Escherichia coli nonhuman nucleotide sequence protein conformation protein structure Pseudomonas aeruginosa species comparison amino acid sequence analogs and derivatives biosynthesis chemistry enzyme active site enzyme specificity enzymology genetics isolation and purification metabolism molecular dynamics Pseudomonas aeruginosa sequence alignment X ray crystallography Bacteria (microorganisms) Escherichia coli Pseudomonas aeruginosa Amino Acid Sequence Bacterial Proteins Binding Sites Catalytic Domain Crystallography, X-Ray Escherichia coli Flavin-Adenine Dinucleotide Molecular Dynamics Simulation NADP Oxidoreductases Potassium Pseudomonas aeruginosa Recombinant Proteins Sequence Alignment Substrate Specificity Uridine Diphosphate N-Acetylglucosamine Chen M.W. Lohkamp B. Schnell R. Lescar J. Schneider G. Substrate Channel Flexibility in Pseudomonas aeruginosa MurB Accommodates Two Distinct Substrates
description	10.1371/journal.pone.0066936
author2	DUKE-NUS MEDICAL SCHOOL
author_facet	DUKE-NUS MEDICAL SCHOOL Chen M.W. Lohkamp B. Schnell R. Lescar J. Schneider G.
format	Article
author	Chen M.W. Lohkamp B. Schnell R. Lescar J. Schneider G.
author_sort	Chen M.W.
title	Substrate Channel Flexibility in Pseudomonas aeruginosa MurB Accommodates Two Distinct Substrates
title_short	Substrate Channel Flexibility in Pseudomonas aeruginosa MurB Accommodates Two Distinct Substrates
title_full	Substrate Channel Flexibility in Pseudomonas aeruginosa MurB Accommodates Two Distinct Substrates
title_fullStr	Substrate Channel Flexibility in Pseudomonas aeruginosa MurB Accommodates Two Distinct Substrates
title_full_unstemmed	Substrate Channel Flexibility in Pseudomonas aeruginosa MurB Accommodates Two Distinct Substrates
title_sort	substrate channel flexibility in pseudomonas aeruginosa murb accommodates two distinct substrates
publisher	Public Library of Science
publishDate	2020
url	https://scholarbank.nus.edu.sg/handle/10635/166195
_version_	1781792008804761600

Substrate Channel Flexibility in Pseudomonas aeruginosa MurB Accommodates Two Distinct Substrates

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