5me4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (18:40, 1 November 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==The structure of HtxB from Pseudomonas stutzeri in complex with hypophosphite to 1.52 A resolution==
==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=''>
+
<StructureSection load='5me4' size='340' side='right'caption='[[5me4]], [[Resolution|resolution]] 1.52&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5me4]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ME4 FirstGlance]. <br>
+
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HP4:phosphinate'>HP4</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]] 1.52&#8491;</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=5me4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5me4 OCA], [http://pdbe.org/5me4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5me4 RCSB], [http://www.ebi.ac.uk/pdbsum/5me4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5me4 ProSAT]</span></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>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/HTXB_PSEST HTXB_PSEST]] Probably forms part of a binding-protein-dependent hypophosphite transporter.
+
[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.
 +
 
 +
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>
 +
 
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 5me4" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Bisson, C]]
+
[[Category: Large Structures]]
-
[[Category: Hitchcock, A]]
+
[[Category: Pseudomonas stutzeri]]
-
[[Category: Abc-transporter]]
+
[[Category: Bisson C]]
-
[[Category: Hypophosphite]]
+
[[Category: Hitchcock A]]
-
[[Category: Periplamic binding protein]]
+
-
[[Category: Phosphite]]
+
-
[[Category: Transport protein]]
+

Current revision

The structure of HtxB from Pseudomonas stutzeri in complex with hypophosphite to 1.52 A resolution

PDB ID 5me4

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools