View source for 4wpy


==Racemic crystal structure of Rv1738 from Mycobacterium tuberculosis (Form-II)==
<StructureSection load='4wpy' size='340' side='right'caption='[[4wpy]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4wpy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WPY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WPY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TFA:TRIFLUOROACETIC+ACID'>TFA</scene></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=4wpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wpy OCA], [https://pdbe.org/4wpy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wpy RCSB], [https://www.ebi.ac.uk/pdbsum/4wpy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wpy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Y1738_MYCTO Y1738_MYCTO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Protein 3D structure can be a powerful predictor of function, but it often faces a critical roadblock at the crystallization step. Rv1738, a protein from Mycobacterium tuberculosis that is strongly implicated in the onset of nonreplicating persistence, and thereby latent tuberculosis, resisted extensive attempts at crystallization. Chemical synthesis of the l- and d-enantiomeric forms of Rv1738 enabled facile crystallization of the d/l-racemic mixture. The structure was solved by an ab initio approach that took advantage of the quantized phases characteristic of diffraction by centrosymmetric crystals. The structure, containing l- and d-dimers in a centrosymmetric space group, revealed unexpected homology with bacterial hibernation-promoting factors that bind to ribosomes and suppress translation. This suggests that the functional role of Rv1738 is to contribute to the shutdown of ribosomal protein synthesis during the onset of nonreplicating persistence of M. tuberculosis.

A functional role of Rv1738 in Mycobacterium tuberculosis persistence suggested by racemic protein crystallography.,Bunker RD, Mandal K, Bashiri G, Chaston JJ, Pentelute BL, Lott JS, Kent SB, Baker EN Proc Natl Acad Sci U S A. 2015 Apr 7;112(14):4310-5. doi:, 10.1073/pnas.1422387112. Epub 2015 Mar 23. PMID:25831534<ref>PMID:25831534</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4wpy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Baker EN]]
[[Category: Bunker RD]]
[[Category: Kent SBH]]
[[Category: Mandal K]]