Crystal Structures of Bacterial Peptidoglycan Amidase AmpD and an Unprecedented Activation Mechanism
Open Access
- 1 September 2011
- journal article
- research article
- Published by Elsevier BV in Journal of Biological Chemistry
- Vol. 286 (36), 31714-31722
- https://doi.org/10.1074/jbc.m111.264366
Abstract
No abstract availableKeywords
This publication has 52 references indexed in Scilit:
- Dali server: conservation mapping in 3DNucleic Acids Research, 2010
- PHENIX: a comprehensive Python-based system for macromolecular structure solutionActa Crystallographica Section D-Structural Biology, 2010
- Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulationThe EMBO Journal, 2009
- Bacterial AmpD at the Crossroads of Peptidoglycan Recycling and Manifestation of Antibiotic ResistanceJournal of the American Chemical Society, 2009
- Total Synthesis of N-Acetylglucosamine-1,6-anhydro-N-acetylmuramylpentapeptide and Evaluation of Its Turnover by AmpD from Escherichia coliJournal of the American Chemical Society, 2009
- Structure of the APPL1 BAR-PH domain and characterization of its interaction with Rab5The EMBO Journal, 2007
- Structural insights into the bactericidal mechanism of human peptidoglycan recognition proteinsProceedings of the National Academy of Sciences of the United States of America, 2007
- CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residuesNucleic Acids Research, 2006
- Coot: model-building tools for molecular graphicsActa Crystallographica Section D-Biological Crystallography, 2004
- A point‐charge force field for molecular mechanics simulations of proteins based on condensed‐phase quantum mechanical calculationsJournal of Computational Chemistry, 2003