2MGV

NMR structure of PASTA domain of PonA2 from Mycobacterium tuberculosis

Summary for 2MGV

• Entry DOI: 10.2210/pdb2mgv/pdb
• NMR Information: BMRB: 19605
• Descriptor: Bifunctional membrane-associated penicillin-binding protein 1A/1B ponA2 (1 entity in total)
• Functional Keywords: pasta domain, penicillin binding protein
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 6578.21

Authors

Calvanese, L.,Falcigno, L.,Maglione, C.,Marasco, D.,Ruggiero, A.,Squeglia, F.,Berisio, R.,D'Auria, G. (deposition date: 2013-11-11, release date: 2013-12-25, Last modification date: 2024-05-15)

Primary citation

Calvanese, L.,Falcigno, L.,Maglione, C.,Marasco, D.,Ruggiero, A.,Squeglia, F.,Berisio, R.,D'Auria, G.
Structural and binding properties of the PASTA domain of PonA2, a key penicillin binding protein from Mycobacterium tuberculosis.
Biopolymers, 101:712-719, 2014

PubMed Abstract: 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 β-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 β-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 β-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.

PubMed: 24281824
DOI: 10.1002/bip.22447

Experimental method

SOLUTION NMR