View source for 7jls


==RV3666c bound to tripeptide==
<StructureSection load='7jls' size='340' side='right'caption='[[7jls]], [[Resolution|resolution]] 1.52&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7jls]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)] and [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=7JLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JLS 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]] 1.52&#8491;</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=7jls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jls OCA], [https://pdbe.org/7jls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jls RCSB], [https://www.ebi.ac.uk/pdbsum/7jls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jls ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/I6X811_MYCTU I6X811_MYCTU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The peptide binding protein DppA is an ABC transporter found in prokaryotes that has the potential to be used as drug delivery tool for hybrid antibiotic compounds. Understanding the motifs and structures that bind to DppA is critical to the development of these bivalent compounds. This study focused on the biophysical analysis of the MtDppA from M. tuberculosis. Analysis of the crystal structure revealed a SVA tripeptide was co-crystallized with the protein. Further peptide analysis demonstrated MtDppA shows very little affinity for dipeptides but rather preferentially binds to peptides that are 3-4 amino acids in length. The structure-activity relationships (SAR) between MtDppA and tripeptides with varied amino acid substitutions were evaluated using thermal shift, SPR, and molecular dynamics simulations. Efforts to identify novel ligands for use as alternative scaffolds through the thermal shift screening of 35,000 compounds against MtDppA were unsuccessful, indicating that the MtDppA binding pocket is highly specialized for uptake of peptides. Future development of compounds that seek to utilize MtDppA as a drug delivery mechanism, will likely require a tri- or tetrapeptide component with a hydrophobic -non-acidic peptide sequence.

Biophysical analysis of the Mycobacteria tuberculosis peptide binding protein DppA reveals a stringent peptide binding pocket.,Fernando DM, Gee CT, Griffith EC, Meyer CJ, Wilt LA, Tangallapally R, Wallace MJ, Miller DJ, Lee RE Tuberculosis (Edinb). 2022 Jan;132:102157. doi: 10.1016/j.tube.2021.102157. Epub , 2021 Nov 29. PMID:34894561<ref>PMID:34894561</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7jls" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Griffith EC]]
[[Category: Lee RE]]
[[Category: Miller DJ]]