Structural and binding properties of the PASTA domain of PonA2, a key penicillin binding protein from Mycobacterium tuberculosis(403 views visite) Calvanese L, Falcigno L, Maglione C, Marasco D, Ruggiero A, Squeglia F, Berisio R, D'Auria G
Keywords Parole chiave: Binding, Structure, Tuberculosis, Antibiotics, Polymers, Proteins, Structure (composition), Antibiotic Binding, Binding Properties, Mycobacterium Tuberculosis, Penicillin- Binding Proteins, Solution Structures, Structural Similarity, Binding Energy, Beta Lactam, Penicillin Binding Protein, Peptidoglycan, Pona2 Protein, Unclassified Drug, Alpha Helix, Article, Carboxy Terminal Sequence, Centrifugation, Complex Formation, Controlled Study, Dormancy, Enzyme Active Site, Heteronuclear Nuclear Magnetic Resonance, Heteronuclear Single Quantum Coherence, Isothermal Titration Calorimetry, Ligand Binding, Nonhuman, Nuclear Overhauser Effect, Pasta Domain, Protein Binding, Protein Conformation, Protein Domain, Protein Expression, Protein Secondary Structure, Sequence Analysis, Surface Plasmon Resonance, Surface Property,
Affiliations Affiliazioni: *** IBB - CNR ***
CIRPeB, University of Naples Federico II, Naples, Italy Department of Pharmacy, University of Naples Federico II, via Mezzocannone 16, 80134 Naples, Italy Institute of Biostructures and Bioimaging-CNR, via Mezzocannone 16, 80134 Naples, Italy Department of Chemical Sciences, University of Naples Federico II, via Cintia 45, 80126 Naples, Italy
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Structural and binding properties of the PASTA domain of PonA2, a key penicillin binding protein from Mycobacterium tuberculosis
PonA2 is one of the two class A penicillin binding proteins of Mycobacterium tuberculosis, the etiologic agent of tuberculosis. It plays a complex role in mycobacterial physiology and is spotted as a promising target for inhibitors. PonA2 is involved in adaptation of M. tuberculosis to dormancy, an ability which has been attributed to the presence in its sequence of a C-terminal PASTA domain. Since PASTA modules are typically considered as beta-lactam antibiotic binding domains, we determined the solution structure of the PASTA domain from PonA2 and analyzed its binding properties versus a plethora of potential binders, including the beta-lactam antibiotics, two typical muropeptide mimics, and polymeric peptidoglycan. We show that, despite a high structural similarity with other PASTA domains, the PASTA domain of PonA2 displays different binding properties, as it is not able to bind muropeptides, or beta-lactams, or polymeric peptidoglycan. These results indicate that the role of PASTA domains cannot be generalized, as their specific binding properties strongly depend on surface residues, which are widely variable. (c) 2013 Wiley Periodicals, Inc. Biopolymers 101: 712-719, 2014.
Structural and binding properties of the PASTA domain of PonA2, a key penicillin binding protein from Mycobacterium tuberculosis
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