2mgv: Difference between revisions
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==NMR structure of PASTA domain of PonA2 from Mycobacterium tuberculosis== | |||
<StructureSection load='2mgv' size='340' side='right' caption='[[2mgv]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2mgv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MGV OCA]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RVBD_3682 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mgv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mgv RCSB], [http://www.ebi.ac.uk/pdbsum/2mgv PDBsum]</span></td></tr> | |||
<table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Myctu]] | |||
[[Category: Auria, G D.]] | [[Category: Auria, G D.]] | ||
[[Category: Berisio, R.]] | [[Category: Berisio, R.]] | ||
Revision as of 06:41, 7 May 2014
NMR structure of PASTA domain of PonA2 from Mycobacterium tuberculosis
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