Crystal Structure of Pseudomonas aeruginosa SPM-1 Provides Insights into Variable Zinc Affinity of Metallo-β-lactamases
about
The Moraxella adhesin UspA1 binds to its human CEACAM1 receptor by a deformable trimeric coiled-coil.Carbapenemases: the versatile beta-lactamasesAsp-120 locates Zn2 for optimal metallo-beta-lactamase activityThe Structure of the Dizinc Subclass B2 Metallo- -Lactamase CphA Reveals that the Second Inhibitory Zinc Ion Binds in the Histidine SiteCrystal structure of New Delhi metallo-β-lactamase reveals molecular basis for antibiotic resistanceCrystal Structures of Pseudomonas aeruginosa GIM-1: Active-Site Plasticity in Metallo- -LactamasesMetallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactionsStructural and biochemical characterization of VIM-26 shows that Leu224 has implications for the substrate specificity of VIM metallo-β-lactamasesThe three-dimensional structure of VIM-31--a metallo-β-lactamase from Enterobacter cloacae in its native and oxidized formStructural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistanceMolecular mechanisms of substrate recognition and specificity of New Delhi metallo-β-lactamaseComputational analysis of pathogen-borne metallo β-lactamases reveals discriminating structural features between B1 types.Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro EvolutionInteraction of Avibactam with Class B Metallo-β-Lactamases.Host-specific enzyme-substrate interactions in SPM-1 metallo-β-lactamase are modulated by second sphere residues.Crystal Structure of DIM-1, an Acquired Subclass B1 Metallo-β-Lactamase from Pseudomonas stutzeri.Crystallization and preliminary diffraction studies of GIM-1, a class B carbapenem-hydrolyzing β-lactamase.B1-Metallo-β-Lactamases: Where Do We Stand?Metallo-β-lactamase structure and function.A variety of roles for versatile zinc in metallo-β-lactamases.In Vitro Antibiofilm Efficacies of Different Antibiotic Combinations with Zinc Sulfate against Pseudomonas aeruginosa Recovered from Hospitalized Patients with Urinary Tract Infection.The mechanisms of catalysis by metallo beta-lactamases.Catalytic role of the metal ion in the metallo-beta-lactamase GOB.Structural Insights into TMB-1 and the Role of Residues 119 and 228 in Substrate and Inhibitor Binding.Role of zinc content on the catalytic efficiency of B1 metallo beta-lactamases.Kinetic characterization of VIM-7, a divergent member of the VIM metallo-beta-lactamase family.19 F-NMR Reveals the Role of Mobile Loops in Product and Inhibitor Binding by the São Paulo Metallo-β-Lactamase.Assay platform for clinically relevant metallo-β-lactamases.Studying the active-site loop movement of the São Paolo metallo-β-lactamase-1†Electronic supplementary information (ESI) available: Procedures for protein expression and purification, 19F-labelling, crystallisation, data collection, and structure deThe CphAII protein from Aquifex aeolicus exhibits a metal-dependent phosphodiesterase activity.Cyclobutanone Mimics of Intermediates in Metallo-β-Lactamase Catalysis.The metallo-beta-lactamase GOB is a mono-Zn(II) enzyme with a novel active site.Shaping substrate selectivity in a broad spectrum metallo-β-lactamase.Exploring the chemistry of penicillin as a beta-lactamase-dependent prodrug.Binding site residues in β-lactamases: role in non-classical interactions and metal binding
P2860
Q24315795-A23CBA3E-9173-4AF7-8003-D9E088EA3D69Q24685034-1687B00F-85B9-4D74-B5C8-4FE668FCCA19Q27644399-7BCDF09D-5E00-4A87-BBD2-84059D260D20Q27656866-3A8EF42E-A1F9-47DB-A998-2F59B196A329Q27670888-4C4330EC-3F00-40C6-8866-B1D2DF7D5A78Q27675349-FFA82AD9-BF17-4412-828B-74AA4C740E1EQ27681358-746383CD-D6A7-4936-82AA-66CF39D67AF6Q27697590-B0A653CC-B649-477C-9B92-472174E0CB2AQ27700062-82D36E76-AE21-468D-9068-FEF94D39DC7EQ28084628-FC492E02-50F3-4F3C-98C9-FC02B2C23F75Q34057408-AAE8A2DA-5620-46CE-848A-AAD0E964A86EQ34158563-3C44AF67-A948-4750-A0BF-3EF51DA389E1Q34418071-A9136615-7EB9-480E-866A-92615A7E0E17Q34533834-113CBB20-A4F7-4ADA-971F-1B96DAA743FFQ35082191-DED92CF3-4AC8-4384-B299-5AC5F4EA392FQ35801593-2740179C-C749-4607-8A7F-33B9E4068BFEQ36398687-B3F0ED0E-D611-41B4-A1EC-774DF44F991EQ36746608-501AEF99-102C-4995-A714-E2954EE47A8BQ38060809-454C91CF-D1D5-408D-BE31-54E8819D458EQ38201660-A80E4CFD-2000-45A2-B924-E21581A40F2EQ38977280-676A647F-1BF8-48A4-9293-CD8ED03AFB90Q39019943-FB7D8492-0934-4E36-B116-245458F87A71Q39541312-2512129D-94BA-43B0-A62C-5A3049E1C788Q40192465-08A975CC-FDDA-41EF-B2B3-067CBB0C7E73Q41129267-B657A44A-9637-4B3A-B7CD-CC15CF75B3D2Q41336218-3612D934-09AB-4010-8C15-5734578D4F9BQ41775520-3CDA7DAB-A0E1-43AB-9174-646161724D4BQ41832679-F88A8B79-8D2F-463B-BBB0-5D4C88516A46Q42103741-6F29F271-7444-4BB6-84BB-73A268B9397CQ43033028-297BC1C9-CE99-4FFB-BA74-186A74CA835CQ46237711-F92D0BF4-C8E4-4E20-8E84-502C431ED503Q48080395-A1D41FCB-C3AF-4274-9238-E5BDE12A678FQ49874620-B531BD66-5872-4373-8588-332E37207D2FQ53582753-51BCC9BC-56E0-4401-A96E-4BA87217A0A8Q57174010-66BED28E-B673-451E-9223-7C2788F63F2D
P2860
Crystal Structure of Pseudomonas aeruginosa SPM-1 Provides Insights into Variable Zinc Affinity of Metallo-β-lactamases
description
im März 2006 veröffentlichter wissenschaftlicher Artikel
@de
scientific article published on 23 January 2006
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в березні 2006
@uk
name
Crystal Structure of Pseudomon ...... finity of Metallo-β-lactamases
@en
Crystal Structure of Pseudomon ...... finity of Metallo-β-lactamases
@nl
type
label
Crystal Structure of Pseudomon ...... finity of Metallo-β-lactamases
@en
Crystal Structure of Pseudomon ...... finity of Metallo-β-lactamases
@nl
prefLabel
Crystal Structure of Pseudomon ...... finity of Metallo-β-lactamases
@en
Crystal Structure of Pseudomon ...... finity of Metallo-β-lactamases
@nl
P2093
P921
P1476
Crystal structure of Pseudomon ...... ity of metallo-beta-lactamases
@en
P2093
Andrea T Hadfield
James Spencer
Lucy E Catto
Stephen E Halford
Tanya A Murphy
P304
P356
10.1016/J.JMB.2006.01.003
P407
P577
2006-01-23T00:00:00Z