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==Solution structure of the N-terminal domain of the Staphylococcus aureus Hibernation Promoting Factor==
<StructureSection load='6qbz' size='340' side='right'caption='[[6qbz]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qbz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QBZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QBZ 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=6qbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qbz OCA], [http://pdbe.org/6qbz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qbz RCSB], [http://www.ebi.ac.uk/pdbsum/6qbz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qbz ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/W8USK0_STAAU W8USK0_STAAU]] Required for dimerization of active 70S ribosomes into 100S ribosomes in stationary phase; 100S ribosomes are translationally inactive and sometimes present during exponential growth.[HAMAP-Rule:MF_00839] 
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== Publication Abstract from PubMed ==
Staphylococcus aureus hibernation promoting factor (SaHPF) is a 22,2 kDa protein which plays a crucial role in 100S Staphylococcus aureus ribosome formation during stress. SaHPF consists of N-terminal domain (NTD) that prevents proteins synthesis by binding to the 30S subunit at the P- and A-sites, connected through a flexible linker with a C-terminal domain (CTD) that keeps ribosomes in 100S form via homodimerization. Recently obtained 100S ribosome structure of S. aureus by cryo-EM shown that SaHPF-NTD bound to the ribosome active sites, however due to the absence of SaHPF-NTD structure it was modeled by homology with the E. coli hibernation factors HPF and YfiA. In present paper we have determined the solution structure of SaHPF-NTD by high-resolution NMR spectroscopy which allows us to increase structural knowledge about HPF structure from S. aureus.

Solution structure of the N-terminal domain of the Staphylococcus aureus hibernation promoting factor.,Usachev KS, Validov SZ, Khusainov IS, Varfolomeev AA, Klochkov VV, Aganov AV, Yusupov MM J Biomol NMR. 2019 May;73(5):223-227. doi: 10.1007/s10858-019-00254-4. Epub 2019 , Jun 4. PMID:31165320<ref>PMID:31165320</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Aganov, A V]]
[[Category: Khusainov, I S]]
[[Category: Klochkov, V V]]
[[Category: Usachev, K S]]
[[Category: Validov, S Z]]
[[Category: Yusupov, M M]]
[[Category: 100s ribosome]]
[[Category: Hibernation promoting factor]]
[[Category: Ribosomal protein]]
[[Category: Staphylococcus aureus]]