6t7o: Difference between revisions
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<StructureSection load='6t7o' size='340' side='right'caption='[[6t7o]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='6t7o' size='340' side='right'caption='[[6t7o]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6t7o]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6t7o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_NCTC_8325 Staphylococcus aureus subsp. aureus NCTC 8325]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5oox 5oox]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T7O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T7O 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]] 1.6000363Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6t7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t7o OCA], [https://pdbe.org/6t7o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t7o RCSB], [https://www.ebi.ac.uk/pdbsum/6t7o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t7o ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/HPF_STAA8 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]<ref>PMID:20015224</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Staphylococcus aureus subsp. aureus NCTC 8325]] | ||
[[Category: Ayupov | [[Category: Ayupov RK]] | ||
[[Category: Fatkhullin | [[Category: Fatkhullin BF]] | ||
[[Category: Gabdulkhakov | [[Category: Gabdulkhakov AG]] | ||
[[Category: Khusainov | [[Category: Khusainov IS]] | ||
[[Category: Tishchenko | [[Category: Tishchenko SV]] | ||
[[Category: Validov | [[Category: Validov SZ]] | ||
[[Category: Yusupov | [[Category: Yusupov MM]] | ||
Latest revision as of 15:56, 24 January 2024
X-ray structure of the C-terminal domain of S. aureus Hibernating Promoting Factor (CTD-SaHPF)X-ray structure of the C-terminal domain of S. aureus Hibernating Promoting Factor (CTD-SaHPF)
Structural highlights
FunctionHPF_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][1] Publication Abstract from PubMedStaphylococcus 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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