4l9e | pdb_00004l9e

Structure of PpsR Q-PAS1 from Rb. sphaeroides

spinqualitylabelsall models 4l9e, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4l9e is a 1 chain structure with sequence from Cereibacter sphaeroides 2.4.1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.65Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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