View source for 6shu


==Borrelia burgdorferi BmpD nucleoside binding protein bound to adenosine==
<StructureSection load='6shu' size='340' side='right'caption='[[6shu]], [[Resolution|resolution]] 1.43&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6shu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi_JD1 Borreliella burgdorferi JD1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SHU 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]] 1.4300287&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=6shu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6shu OCA], [https://pdbe.org/6shu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6shu RCSB], [https://www.ebi.ac.uk/pdbsum/6shu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6shu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BMPD_BORBU BMPD_BORBU] Binds adenosine and inosine but not guanosine, xanthosine or ribose (PubMed:31988175). May be part of an ABC-type nucleoside uptake system involved in the purine salvage pathway (Probable) (PubMed:31988175). Other probable members of the ABC transporter system are substrate binding proteins BmpB, BmpA and BmpC (BB_0382, BB_0383 and BB_0384 respectively), ATP transporter RbsA and 2 permeases (BB_0677, BB_0678 and BB_0679 respectively) (Probable) (PubMed:31988175).<ref>PMID:31988175</ref> <ref>PMID:31988175</ref> 
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== Publication Abstract from PubMed ==
Borrelia burgdorferi sensu lato (sl), the causative agent of the tick-borne Lyme borreliosis (LB), has a limited metabolic capacity and needs to acquire nutrients, such as amino acids, fatty acids, and nucleic acids, from the host environment. Using X-ray crystallography, liquid chromatography-mass spectrometry, microscale thermophoresis, and cellular localization studies, we show that Basic membrane protein D (BmpD) is a periplasmic substrate-binding protein of an ABC transporter system binding to purine nucleosides. Nucleosides are essential for bacterial survival in the host organism and these studies suggest a key role for BmpD in the purine salvage pathway of B. burgdorferi sl. As B. burgdorferi sl lacks the enzymes required for de novo purine synthesis, BmpD may play a vital role in ensuring access to the purines needed for sustaining an infection in the host. Further, we show that although human LB patients develop anti-BmpD antibodies, immunization of mice with BmpD does not confer protection against B. burgdorferi sl infection.

Structural and biomolecular analyses of Borrelia burgdorferi BmpD reveal a substrate-binding protein of an ABC-type nucleoside transporter family.,Cuellar J, Astrand M, Elovaara H, Pietikainen A, Siren S, Liljeblad A, Guedez G, Salminen TA, Hytonen J Infect Immun. 2020 Jan 27. pii: IAI.00962-19. doi: 10.1128/IAI.00962-19. PMID:31988175<ref>PMID:31988175</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6shu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Borreliella burgdorferi JD1]]
[[Category: Large Structures]]
[[Category: Astrand M]]
[[Category: Cuellar J]]
[[Category: Guedez G]]
[[Category: Hytonen J]]
[[Category: Salminen TA]]