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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6T7O FirstGlance]. <br> | <table><tr><td colspan='2'>[[6t7o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staa8 Staa8]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6T7O FirstGlance]. <br> | ||
</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=6t7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t7o OCA], [http://pdbe.org/6t7o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t7o RCSB], [http://www.ebi.ac.uk/pdbsum/6t7o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t7o ProSAT]</span></td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hpf, SAOUHSC_00767 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=93061 STAA8])</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=6t7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t7o OCA], [http://pdbe.org/6t7o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t7o RCSB], [http://www.ebi.ac.uk/pdbsum/6t7o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t7o ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Staa8]] | |||
[[Category: Ayupov, R K]] | [[Category: Ayupov, R K]] | ||
[[Category: Fatkhullin, B F]] | [[Category: Fatkhullin, B F]] | ||
Revision as of 19:55, 22 January 2020
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
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][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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