Solution structure of the N-terminal domain of the Staphylococcus aureus hibernation promoting factor.

Abstract:

: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.

journal_name

J Biomol NMR

authors

Usachev KS,Validov SZ,Khusainov IS,Varfolomeev AA,Klochkov VV,Aganov AV,Yusupov MM

doi

10.1007/s10858-019-00254-4

subject

Has Abstract

pub_date

2019-05-01 00:00:00

pages

223-227

issue

5

eissn

0925-2738

issn

1573-5001

pii

10.1007/s10858-019-00254-4

journal_volume

73

pub_type

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