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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4dz3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_pseudomallei_1710b Burkholderia pseudomallei 1710b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DZ3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4dz3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_pseudomallei_1710b Burkholderia pseudomallei 1710b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DZ3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FK5:8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN'>FK5</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FK5:8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN'>FK5</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=4dz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dz3 OCA], [https://pdbe.org/4dz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dz3 RCSB], [https://www.ebi.ac.uk/pdbsum/4dz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dz3 ProSAT]</span></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=4dz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dz3 OCA], [https://pdbe.org/4dz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dz3 RCSB], [https://www.ebi.ac.uk/pdbsum/4dz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dz3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/Q3JK38_BURP1 Q3JK38_BURP1]]
[https://www.uniprot.org/uniprot/Q3JK38_BURP1 Q3JK38_BURP1]  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Macrophage infectivity potentiators (Mips) are immunophilin proteins and essential virulence factors for a range of pathogenic organisms. We applied a structural biology approach to characterize a Mip from Burkholderia pseudomallei (BpML1), the causative agent of melioidosis. Crystal structure and nuclear magnetic resonance analyses of BpML1 in complex with known macrocyclics and other derivatives led to the identification of a key chemical scaffold. This scaffold possesses inhibitory potency for BpML1 without the immunosuppressive components of related macrocyclic agents. Biophysical characterization of a compound series with this scaffold allowed binding site specificity in solution and potency determinations for rank ordering the set. The best compounds in this series possessed a low-micromolar affinity for BpML1, bound at the site of enzymatic activity, and inhibited a panel of homologous Mip proteins from other pathogenic bacteria, without demonstrating toxicity in human macrophages. Importantly, the in vitro activity of BpML1 was reduced by these compounds, leading to decreased macrophage infectivity and intracellular growth of Burkholderia pseudomallei. These compounds offer the potential for activity against a new class of antimicrobial targets and present the utility of a structure-based approach for novel antimicrobial drug discovery.
 
A structural biology approach enables the development of antimicrobials targeting bacterial immunophilins.,Begley DW, Fox D 3rd, Jenner D, Juli C, Pierce PG, Abendroth J, Muruthi M, Safford K, Anderson V, Atkins K, Barnes SR, Moen SO, Raymond AC, Stacy R, Myler PJ, Staker BL, Harmer NJ, Norville IH, Holzgrabe U, Sarkar-Tyson M, Edwards TE, Lorimer DD Antimicrob Agents Chemother. 2014 Mar;58(3):1458-67. doi: 10.1128/AAC.01875-13., Epub 2013 Dec 23. PMID:24366729<ref>PMID:24366729</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4dz3" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Burkholderia pseudomallei 1710b]]
[[Category: Burkholderia pseudomallei 1710b]]
[[Category: Large Structures]]
[[Category: Large Structures]]

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