View source for 2mgv


==NMR structure of PASTA domain of PonA2 from Mycobacterium tuberculosis==
<StructureSection load='2mgv' size='340' side='right'caption='[[2mgv]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mgv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MGV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MGV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mgv OCA], [https://pdbe.org/2mgv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mgv RCSB], [https://www.ebi.ac.uk/pdbsum/2mgv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mgv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/I6YGX2_MYCTU I6YGX2_MYCTU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 analysed 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, nor beta-lactams, nor 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.

Structural and binding properties of the PASTA domain of PonA2, a key penicillin binding protein from Mycobacterium tuberculosis.,Calvanese L, Falcigno L, Maglione C, Marasco D, Ruggiero A, Squeglia F, Berisio R, D'Auria G Biopolymers. 2013 Nov 27. doi: 10.1002/bip.22447. PMID:24281824<ref>PMID:24281824</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mgv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Berisio R]]
[[Category: Calvanese L]]
[[Category: D'Auria G]]
[[Category: Falcigno L]]
[[Category: Maglione C]]
[[Category: Marasco D]]
[[Category: Ruggiero A]]
[[Category: Squeglia F]]