View source for 6wce


==Structure of the periplasmic binding protein P5PA==
<StructureSection load='6wce' size='340' side='right'caption='[[6wce]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6wce]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinobacillus_pleuropneumoniae Actinobacillus pleuropneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WCE 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]] 1.754&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=6wce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wce OCA], [https://pdbe.org/6wce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wce RCSB], [https://www.ebi.ac.uk/pdbsum/6wce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wce ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B0BUC2_ACTPJ B0BUC2_ACTPJ] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacteria require high efficiency uptake systems to survive and proliferate in nutrient limiting environments, such as those found in host organisms. ATP binding cassette (ABC) transporters in the bacterial plasma membrane provide a mechanism for transport of many substrates. In this study, we examine an operon containing a periplasmic binding protein in Actinobacillus for its potential role in nutrient acquisition. The 1.76 A resolution electron density map obtained from the crystal structure of the periplasmic binding protein was best fit with a molecular model containing a pyridoxal-5'-phosphate (P5P/PLP/the active form of vitamin B6) ligand within the protein's binding site. The identity of the P5P bound to this periplasmic binding protein was verified by isothermal titration calorimetry, microscale thermophoresis, and mass spectrometry, leading us to name the protein P5PA and the operon P5PAB. To illustrate the functional utility of this uptake system, we introduced the P5PAB operon from A. pleuropneumoniae into an E. coli K-12 strain that was devoid of a key enzyme required for P5P synthesis. The growth of this strain at low levels of P5P supports the functional role of this operon in P5P uptake. This is the first report of a dedicated P5P bacterial uptake system, but through bioinformatics we discovered homologs mainly within pathogenic representatives of the Pasteurellaceae family, suggesting that this operon exists more widely outside the Actinobacillus genus.

Actinobacillus utilizes a binding-protein dependent ABC transporter to acquire the active form of Vitamin B6.,Pan C, Zimmer A, Shah M, Huynh MS, Chieh-Lin Lai C, Sit B, Hooda Y, Curran DM, Moraes TF J Biol Chem. 2021 Aug 3:101046. doi: 10.1016/j.jbc.2021.101046. PMID:34358566<ref>PMID:34358566</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6wce" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Actinobacillus pleuropneumoniae]]
[[Category: Large Structures]]
[[Category: Hooda Y]]
[[Category: Huynh M]]
[[Category: Lai CCL]]
[[Category: Moraes TF]]
[[Category: Pan C]]
[[Category: Shah M]]
[[Category: Sit B]]
[[Category: Zimmer A]]