1sw5: Difference between revisions
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<StructureSection load='1sw5' size='340' side='right'caption='[[1sw5]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1sw5' size='340' side='right'caption='[[1sw5]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1sw5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1sw5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_DSM_4304 Archaeoglobus fulgidus DSM 4304]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SW5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SW5 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1sw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sw5 OCA], [https://pdbe.org/1sw5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sw5 RCSB], [https://www.ebi.ac.uk/pdbsum/1sw5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sw5 ProSAT]</span></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=1sw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sw5 OCA], [https://pdbe.org/1sw5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sw5 RCSB], [https://www.ebi.ac.uk/pdbsum/1sw5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sw5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/O29280_ARCFU O29280_ARCFU] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Archaeoglobus fulgidus DSM 4304]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bremer | [[Category: Bremer E]] | ||
[[Category: Diederichs | [[Category: Diederichs K]] | ||
[[Category: Holtmann | [[Category: Holtmann G]] | ||
[[Category: Schiefner | [[Category: Schiefner A]] | ||
[[Category: Welte | [[Category: Welte W]] | ||
Latest revision as of 09:21, 23 August 2023
Crystal structure of ProX from Archeoglobus fulgidus in the ligand free formCrystal structure of ProX from Archeoglobus fulgidus in the ligand free form
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCompatible solutes such as glycine betaine and proline betaine serve as protein stabilizers because of their preferential exclusion from protein surfaces. To use extracellular sources of this class of compounds as osmo-, cryo-, or thermoprotectants, Bacteria and Archaea have developed high affinity uptake systems of the ATP-binding cassette type. These transport systems require periplasmic- or extracellular-binding proteins that are able to bind the transported substance with high affinity. Therefore, binding proteins that bind compatible solutes have to avoid the exclusion of their ligands within the binding pocket. In the present study we addressed the question to how compatible solutes can be effectively bound by a protein at temperatures around 83 degrees C as this is done by the ligand-binding protein ProX from the hyperthermophilic archaeon Archaeoglobus fulgidus. We solved the structures of ProX without ligand and in complex with both of its natural ligands glycine betaine and proline betaine, as well as in complex with the artificial ligand trimethylammonium. Cation-pi interactions and non-classical hydrogen bonds between four tyrosine residues, a main chain carbonyl oxygen, and the ligand have been identified to be the key determinants in binding the quaternary amines of the three investigated ligands. The comparison of the ligand binding sites of ProX from A. fulgidus and the recently solved structure of ProX from Escherichia coli revealed a very similar solution for the problem of compatible solute binding, although both proteins share only a low degree of sequence identity. The residues involved in ligand binding are functionally equivalent but not conserved in the primary sequence. Structural basis for the binding of compatible solutes by ProX from the hyperthermophilic archaeon Archaeoglobus fulgidus.,Schiefner A, Holtmann G, Diederichs K, Welte W, Bremer E J Biol Chem. 2004 Nov 12;279(46):48270-81. Epub 2004 Aug 11. PMID:15308642[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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