6ghq: Difference between revisions
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==HtxB D206N protein variant from Pseudomonas stutzeri in a partially open conformation to 1.53 A resolution== | |||
<StructureSection load='6ghq' size='340' side='right'caption='[[6ghq]], [[Resolution|resolution]] 1.53Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ghq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"achromobacter_sewerinii"_bergey_et_al._1923 "achromobacter sewerinii" bergey et al. 1923]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GHQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GHQ FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6emn|6emn]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">htxB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=316 "Achromobacter sewerinii" Bergey et al. 1923])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ghq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ghq OCA], [http://pdbe.org/6ghq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ghq RCSB], [http://www.ebi.ac.uk/pdbsum/6ghq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ghq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/HTXB_PSEST HTXB_PSEST]] Probably forms part of a binding-protein-dependent hypophosphite transporter. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Phosphorus acquisition is critical for life. In low phosphate conditions, some species of bacteria have evolved mechanisms to import reduced phosphorus compounds, such as phosphite and hypophosphite, as alternative phosphorus sources. Uptake is facilitated by high-affinity periplasmic binding proteins (PBPs) that bind cargo in the periplasm and shuttle it to an ATP-binding cassette (ABC)-transporter in the bacterial inner membrane. PtxB and HtxB are the PBPs responsible for binding phosphite and hypophosphite, respectively. They recognize the P-H bond of phosphite/hypophosphite via a conserved P-H...pi interaction, which confers nanomolar dissociation constants for their respective ligands. PtxB also has a low-level binding affinity for phosphate and hypophosphite, whilst HtxB can facilitate phosphite uptake in vivo. However, HtxB does not bind phosphate, thus the HtxBCDE transporter has recently been successfully exploited for biocontainment of genetically modified organisms by phosphite-dependent growth. Here we use a combination of X-ray crystallography, NMR and Microscale Thermophoresis to show that phosphite binding to HtxB depends on the protonation state of the ligand, suggesting that pH may effect the efficiency of phosphite uptake by HtxB in biotechnology applications. | |||
Phosphite binding by the HtxB periplasmic binding protein depends on the protonation state of the ligand.,Adams NBP, Robertson AJ, Hunter CN, Hitchcock A, Bisson C Sci Rep. 2019 Jul 15;9(1):10231. doi: 10.1038/s41598-019-46557-2. PMID:31308436<ref>PMID:31308436</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6ghq" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Achromobacter sewerinii bergey et al. 1923]] | |||
[[Category: Large Structures]] | |||
[[Category: Adams, N B]] | |||
[[Category: Bisson, C]] | |||
[[Category: Hitchcock, A]] | |||
[[Category: Robertson, A J]] | |||
[[Category: Abc-transporter]] | |||
[[Category: Hypophosphite]] | |||
[[Category: Periplasmic binding protein]] | |||
[[Category: Phosphite]] | |||
[[Category: Transport protein]] | |||
Latest revision as of 11:33, 24 July 2019
HtxB D206N protein variant from Pseudomonas stutzeri in a partially open conformation to 1.53 A resolutionHtxB D206N protein variant from Pseudomonas stutzeri in a partially open conformation to 1.53 A resolution
Structural highlights
Function[HTXB_PSEST] Probably forms part of a binding-protein-dependent hypophosphite transporter. Publication Abstract from PubMedPhosphorus acquisition is critical for life. In low phosphate conditions, some species of bacteria have evolved mechanisms to import reduced phosphorus compounds, such as phosphite and hypophosphite, as alternative phosphorus sources. Uptake is facilitated by high-affinity periplasmic binding proteins (PBPs) that bind cargo in the periplasm and shuttle it to an ATP-binding cassette (ABC)-transporter in the bacterial inner membrane. PtxB and HtxB are the PBPs responsible for binding phosphite and hypophosphite, respectively. They recognize the P-H bond of phosphite/hypophosphite via a conserved P-H...pi interaction, which confers nanomolar dissociation constants for their respective ligands. PtxB also has a low-level binding affinity for phosphate and hypophosphite, whilst HtxB can facilitate phosphite uptake in vivo. However, HtxB does not bind phosphate, thus the HtxBCDE transporter has recently been successfully exploited for biocontainment of genetically modified organisms by phosphite-dependent growth. Here we use a combination of X-ray crystallography, NMR and Microscale Thermophoresis to show that phosphite binding to HtxB depends on the protonation state of the ligand, suggesting that pH may effect the efficiency of phosphite uptake by HtxB in biotechnology applications. Phosphite binding by the HtxB periplasmic binding protein depends on the protonation state of the ligand.,Adams NBP, Robertson AJ, Hunter CN, Hitchcock A, Bisson C Sci Rep. 2019 Jul 15;9(1):10231. doi: 10.1038/s41598-019-46557-2. PMID:31308436[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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