Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme
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Carbapenemases: the versatile beta-lactamasesProbing substrate binding to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia by using site-directed mutagenesisSolving nucleic acid structures by molecular replacement: examples from group II intron studiesStructural effects of the active site mutation cysteine to serine inBacillus cereuszinc-β-lactamaseCrystal structure of D-aminoacylase from Alcaligenes faecalis DA1. A novel subset of amidohydrolases and insights into the enzyme mechanismAsp-120 locates Zn2 for optimal metallo-beta-lactamase activityAdaptive protein evolution grants organismal fitness by improving catalysis and flexibilityHigh-Resolution Crystal Structure of the Subclass B3 Metallo- -Lactamase BJP-1: Rational Basis for Substrate Specificity and Interaction with SulfonamidesStructure of Apo- and Monometalated Forms of NDM-1—A Highly Potent Carbapenem-Hydrolyzing Metallo-β-LactamaseSolution structures of the Bacillus cereus metallo-β-lactamase BcII and its complex with the broad spectrum inhibitor R -thiomandelic acidMetallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactionsUse of ferrous iron by metallo-β-lactamasesOvercoming differences: The catalytic mechanism of metallo-β-lactamasesIdentification of residues critical for metallo-beta-lactamase function by codon randomization and selectionDetection and sequence/structure mapping of biophysical constraints to protein variation in saturated mutational libraries and protein sequence alignments with a dedicated serverMimicking natural evolution in metallo-beta-lactamases through second-shell ligand mutations.beta-Lactamase epidemiology and the utility of established and novel beta-lactamase inhibitors.Complete ¹H, ¹⁵N, and ¹³C resonance assignments of Bacillus cereus metallo-β-lactamase and its complex with the inhibitor R-thiomandelic acid.Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro EvolutionThe crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa, defines a third class of sulfatasesHost-specific enzyme-substrate interactions in SPM-1 metallo-β-lactamase are modulated by second sphere residues.Plasmids from the gut microbiome of cabbage root fly larvae encode SaxA that catalyses the conversion of the plant toxin 2-phenylethyl isothiocyanate.Crystal Structure of DIM-1, an Acquired Subclass B1 Metallo-β-Lactamase from Pseudomonas stutzeri.Differential binding of Co(II) and Zn(II) to metallo-beta-lactamase Bla2 from Bacillus anthracis.Grafting a new metal ligand in the cocatalytic site of B. cereus metallo-beta-lactamase: structural flexibility without loss of activity.X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus.Probing the role of Met221 in the unusual metallo-β-lactamase GOB-18.B1-Metallo-β-Lactamases: Where Do We Stand?Engineered mononuclear variants in Bacillus cereus metallo-beta-lactamase BcII are inactive.Folding strategy to prepare Co(II)-substituted metallo-beta-lactamase L1.Metallo beta lactamases in Pseudomonas aeruginosa and Acinetobacter species.Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1Crystal Structure of the Metallo-β-Lactamase GOB in the Periplasmic Dizinc Form Reveals an Unusual Metal Site.Metallo-β-lactamase structure and function.A variety of roles for versatile zinc in metallo-β-lactamases.Functional control of the binuclear metal site in the metallo-beta-lactamase-like fold by subtle amino acid replacements.Characterization of monomeric L1 metallo-beta -lactamase and the role of the N-terminal extension in negative cooperativity and antibiotic hydrolysis.Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by site-directed mutagenesis.Potential inhibitors designed against NDM-1 type metallo-β-lactamases: an attempt to enhance efficacies of antibiotics against multi-drug-resistant bacteriaThe mechanisms of catalysis by metallo beta-lactamases.
P2860
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P2860
Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme
description
1998 nî lūn-bûn
@nan
1998 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Crystal structure of the zinc- ...... atures of a mononuclear enzyme
@ast
Crystal structure of the zinc- ...... atures of a mononuclear enzyme
@en
Crystal structure of the zinc- ...... atures of a mononuclear enzyme
@nl
type
label
Crystal structure of the zinc- ...... atures of a mononuclear enzyme
@ast
Crystal structure of the zinc- ...... atures of a mononuclear enzyme
@en
Crystal structure of the zinc- ...... atures of a mononuclear enzyme
@nl
prefLabel
Crystal structure of the zinc- ...... atures of a mononuclear enzyme
@ast
Crystal structure of the zinc- ...... atures of a mononuclear enzyme
@en
Crystal structure of the zinc- ...... atures of a mononuclear enzyme
@nl
P2093
P3181
P356
P1433
P1476
Crystal structure of the zinc- ...... atures of a mononuclear enzyme
@en
P2093
B J Sutton
J H Bateson
S M Fabiane
T Mitchell
P304
P3181
P356
10.1021/BI980506I
P407
P577
1998-09-08T00:00:00Z