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| | ==Structure of a SeMet derivative of PpsR Q-PAS1 from Rb. sphaeroides== | | ==Structure of a SeMet derivative of PpsR Q-PAS1 from Rb. sphaeroides== |
| - | <StructureSection load='4l9f' size='340' side='right' caption='[[4l9f]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='4l9f' size='340' side='right'caption='[[4l9f]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4l9f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhos4 Rhos4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L9F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L9F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4l9f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides_2.4.1 Cereibacter sphaeroides 2.4.1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L9F FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hh2|4hh2]], [[4hh3|4hh3]], [[4hh0|4hh0]], [[4l9e|4l9e]], [[4l9g|4l9g]]</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=4l9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l9f OCA], [https://pdbe.org/4l9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l9f RCSB], [https://www.ebi.ac.uk/pdbsum/4l9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l9f ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ppsR, RHOS4_18870, RSP_0282 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272943 RHOS4])</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=4l9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l9f OCA], [http://pdbe.org/4l9f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4l9f RCSB], [http://www.ebi.ac.uk/pdbsum/4l9f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4l9f ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q3J179_CERS4 Q3J179_CERS4] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Rhos4]] | + | [[Category: Cereibacter sphaeroides 2 4.1]] |
| - | [[Category: Heintz, U]] | + | [[Category: Large Structures]] |
| - | [[Category: Meinhart, A]] | + | [[Category: Heintz U]] |
| - | [[Category: Schlichting, I]] | + | [[Category: Meinhart A]] |
| - | [[Category: Winkler, A]] | + | [[Category: Schlichting I]] |
| - | [[Category: Oligomerization]]
| + | [[Category: Winkler A]] |
| - | [[Category: Pas domain]]
| + | |
| - | [[Category: Per-arnt-sim]]
| + | |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
Q3J179_CERS4
Publication Abstract from PubMed
Per-ARNT-Sim (PAS) domains are essential modules of many multi-domain signalling proteins that mediate protein interaction and/or sense environmental stimuli. Frequently, multiple PAS domains are present within single polypeptide chains, where their interplay is required for protein function. Although many isolated PAS domain structures have been reported over the last decades, only a few structures of multi-PAS proteins are known. Therefore, the molecular mechanism of multi-PAS domain-mediated protein oligomerization and function is poorly understood. The transcription factor PpsR from Rhodobacter sphaeroides is such a multi-PAS domain protein that, in addition to its three PAS domains, contains a glutamine-rich linker and a C-terminal helix-turn-helix DNA-binding motif. Here, crystal structures of two N-terminally and C-terminally truncated PpsR variants that comprise a single (PpsRQ-PAS1) and two (PpsRN-Q-PAS1) PAS domains, respectively, are presented and the multi-step strategy required for the phasing of a triple PAS domain construct (PpsRDeltaHTH) is illustrated. While parts of the biologically relevant dimerization interface can already be observed in the two shorter constructs, the PpsRDeltaHTH structure reveals how three PAS domains enable the formation of multiple oligomeric states (dimer, tetramer and octamer), highlighting that not only the PAS cores but also their alpha-helical extensions are essential for protein oligomerization. The results demonstrate that the long helical glutamine-rich linker of PpsR results from a direct fusion of the N-cap of the PAS1 domain with the C-terminal extension of the N-domain that plays an important role in signal transduction.
Multi-PAS domain-mediated protein oligomerization of PpsR from Rhodobacter sphaeroides.,Heintz U, Meinhart A, Winkler A Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):863-76. doi:, 10.1107/S1399004713033634. Epub 2014 Feb 27. PMID:24598755[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Heintz U, Meinhart A, Winkler A. Multi-PAS domain-mediated protein oligomerization of PpsR from Rhodobacter sphaeroides. Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):863-76. doi:, 10.1107/S1399004713033634. Epub 2014 Feb 27. PMID:24598755 doi:http://dx.doi.org/10.1107/S1399004713033634
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