6t7o

X-ray structure of the C-terminal domain of S. aureus Hibernating Promoting Factor (CTD-SaHPF)

spinqualitylabelsall models 6t7o, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6t7o is a 2 chain structure with sequence from Staphylococcus aureus subsp. aureus NCTC 8325. This structure supersedes the now removed PDB entry 5oox. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6000363Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HPF_STAA8 Required for dimerization of active 70S ribosomes into 100S ribosomes; when added to monomeric 70S ribosomes stimulates formation of 100S dimeric ribosomes. Unlike E.coli, 100S ribosomes are present during exponential growth, peak during early stationary phase and then decrease (shown for strain NBRC 3060).[HAMAP-Rule:MF_00839] Publication Abstract from PubMed Staphylococcus aureus hibernation promoting factor (SaHPF) is responsible for the formation of 100S ribosome dimers, which in turn help this pathogen to reduce energy spent under unfavorable conditions. Ribosome dimer formation strongly depends on the dimerization of the C-terminal domain of SaHPF (CTD(SaHPF)). In this study, we solved the crystal structure of CTD(SaHPF) at 1.6A resolution and obtained a precise arrangement of the dimer interface. Residues Phe(160), Val(162), Thr(171), Ile(173), Tyr(175), Ile(185) andThr(187) in the dimer interface of SaHPF protein were mutated and the effects were analyzed for the formation of 100S disomes of ribosomes isolated from S. aureus. It was shown that substitution of any of single residues Phe(160), Val(162), Ile(173), Tyr(175) and Ile(185) in the SaHPF homodimer interface abolished the ribosome dimerization in vitro. Dimerization of long hibernation promoting factor from Staphylococcus aureus: Structural analysis and biochemical characterization.,Usachev KS, Fatkhullin BF, Klochkova EA, Miftakhov AK, Golubev AA, Bikmullin AG, Nurullina LI, Garaeva NS, Islamov DR, Gabdulkhakov AG, Lekontseva NV, Tishchenko SV, Balobanov VA, Khusainov IS, Yusupov MM, Validov SZ J Struct Biol. 2019 Oct 25:107408. doi: 10.1016/j.jsb.2019.107408. PMID:31669310 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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