Mutagenesis of Zinc Ligand Residue Cys221 Reveals Plasticity in the IMP-1 Metallo- -Lactamase Active Site - Test2 - elhamkhani - TriplyDB

Mutagenesis of Zinc Ligand Residue Cys221 Reveals Plasticity in the IMP-1 Metallo- -Lactamase Active Site

Mutagenesis of Zinc Ligand Residue Cys221 Reveals Plasticity in the IMP-1 Metallo- -Lactamase Active Site

http://www.wikidata.org/entity/Q27671609

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Iron(III) located in the dinuclear metallo-β-lactamase IMP-1 by pseudocontact shifts Biochemical characterization of New Delhi metallo-β-lactamase variants reveals differences in protein stability.An altered zinc-binding site confers resistance to a covalent inactivator of New Delhi metallo-beta-lactamase-1 (NDM-1) discovered by high-throughput screening Deep Sequencing of Random Mutant Libraries Reveals the Active Site of the Narrow Specificity CphA Metallo-β-Lactamase is Fragile to Mutations.B1-Metallo-β-Lactamases: Where Do We Stand?Metallo-β-lactamase structure and function.Understanding the determinants of substrate specificity in IMP family metallo-β-lactamases: the importance of residue 262.Binding site residues in β-lactamases: role in non-classical interactions and metal binding Differential active site requirements for NDM-1 β-lactamase hydrolysis of carbapenem versus penicillin and cephalosporin antibiotics

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P2860

Mutagenesis of Zinc Ligand Residue Cys221 Reveals Plasticity in the IMP-1 Metallo- -Lactamase Active Site

http://www.wikidata.org/entity/Q27671609

description

2012 nî lūn-bûn

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2012 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2012 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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Mutagenesis of Zinc Ligand Res ...... etallo- -Lactamase Active Site

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Mutagenesis of Zinc Ligand Res ...... etallo- -Lactamase Active Site

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Antimicrobial Agents and Chemotherapy

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Mutagenesis of Zinc Ligand Res ...... etallo- -Lactamase Active Site

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B V Venkataram Prasad

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Ernest Lykissa

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Kevin J Phillips

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Lori B Horton

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Nicholas G Brown

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Rose Mikulski

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Sreejesh Shanker

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Timothy Palzkill

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P2860

Updated functional classification of beta-lactamases

For the record: Structural consequences of the active site substitution Cys181 → Ser in metallo-β-lactamase from bacteroides fragilis

Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor

The structural bases of antibiotic resistance in the clinically derived mutant beta-lactamases TEM-30, TEM-32, and TEM-34

Structural basis for the role of Asp-120 in metallo-beta-lactamases

The Zn2 position in metallo-beta-lactamases is critical for activity: a study on chimeric metal sites on a conserved protein scaffold

Genetic and Structural Characterization of an L201P Global Suppressor Substitution in TEM-1 β-Lactamase

The Structure of the Dizinc Subclass B2 Metallo- -Lactamase CphA Reveals that the Second Inhibitory Zinc Ion Binds in the Histidine Site

Structural Analysis of Histo-Blood Group Antigen Binding Specificity in a Norovirus GII.4 Epidemic Variant: Implications for Epochal Evolution

The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution

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5667-77

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scholarly article

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10.1128/AAC.01276-12

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11

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56

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2012-11-01T00:00:00Z

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22908171

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3486559

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