5me4: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 5me4 is ON HOLD
+==The structure of HtxB from Pseudomonas stutzeri in complex with hypophosphite to 1.52 A resolution==
+<StructureSection load='5me4' size='340' side='right'caption='[[5me4]], [[Resolution|resolution]] 1.52&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5me4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ME4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ME4 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HP4:phosphinate'>HP4</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=5me4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5me4 OCA], [https://pdbe.org/5me4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5me4 RCSB], [https://www.ebi.ac.uk/pdbsum/5me4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5me4 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HTXB_STUST HTXB_STUST] Probably forms part of a binding-protein-dependent hypophosphite transporter.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Inorganic phosphate is the major bioavailable form of the essential nutrient phosphorus. However, the concentration of phosphate in most natural habitats is low enough to limit microbial growth. Under phosphate-depleted conditions some bacteria utilise phosphite and hypophosphite as alternative sources of phosphorus, but the molecular basis of reduced phosphorus acquisition from the environment is not fully understood. Here, we present crystal structures and ligand binding affinities of periplasmic binding proteins from bacterial phosphite and hypophosphite ATP-binding cassette transporters. We reveal that phosphite and hypophosphite specificity results from a combination of steric selection and the presence of a P-H...pi interaction between the ligand and a conserved aromatic residue in the ligand-binding pocket. The characterisation of high affinity and specific transporters has implications for the marine phosphorus redox cycle, and might aid the use of phosphite as an alternative phosphorus source in biotechnological, industrial and agricultural applications.
-Authors:
+The molecular basis of phosphite and hypophosphite recognition by ABC-transporters.,Bisson C, Adams NBP, Stevenson B, Brindley AA, Polyviou D, Bibby TS, Baker PJ, Hunter CN, Hitchcock A Nat Commun. 2017 Nov 23;8(1):1746. doi: 10.1038/s41467-017-01226-8. PMID:29170493<ref>PMID:29170493</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5me4" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Pseudomonas stutzeri]]
+[[Category: Bisson C]]
+[[Category: Hitchcock A]]