V
Vladimir A. Meshcheryakov
Researcher at Okinawa Institute of Science and Technology
Publications - 18
Citations - 331
Vladimir A. Meshcheryakov is an academic researcher from Okinawa Institute of Science and Technology. The author has contributed to research in topics: Transmembrane domain & Aquifex aeolicus. The author has an hindex of 8, co-authored 18 publications receiving 275 citations. Previous affiliations of Vladimir A. Meshcheryakov include Russian Academy of Sciences & National University of Singapore.
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Journal ArticleDOI
MmpL3 is the flippase for mycolic acids in mycobacteria
TL;DR: This study established the role of an essential membrane protein as the flippase for MAs and demonstrated that this protein is a direct target of an antimycobacterial compound and provides fundamental insights into OM biogenesis and MA transport in mycobacteria.
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Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteins.
Roman Fedorov,Vladimir A. Meshcheryakov,G.M. Gongadze,N.P. Fomenkova,N. Nevskaya,Maria Selmer,Martin Laurberg,Ole Kristensen,Salam Al-Karadaghi,Anders Liljas,Maria Garber,Stanislav Nikonov +11 more
TL;DR: The crystal structure of Thermus thermophilus ribosomal protein TL5 in complex with a fragment of Escherichia coli 5S rRNA has been determined and the TL5 sequence reveals homology to the so-called general stress protein CTC.
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Inhibition of a type III secretion system by the deletion of a short loop in one of its membrane proteins
TL;DR: The deletion of a short loop in the cytoplasmic domain of Salmonella FlhB completely abolishes secretion by the type III secretion system and a molecular-dynamics simulation shows that the deletion of the loop affects the flexibility of a linker between the transmembrane and cytop lasmic domains of Flh B.
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High‐resolution archaellum structure reveals a conserved metal‐binding site
Vladimir A. Meshcheryakov,Satoshi Shibata,Makoto Schreiber,Alejandro Villar-Briones,Ken F. Jarrell,Shin-Ichi Aizawa,Matthias Wolf +6 more
TL;DR: It is shown in vitro that the metal‐binding site, which appears to be a widespread property of archaellin, is required for filament integrity, and identified N‐linked glycosylation by cryo‐EM and mass spectrometry.
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N-terminal domain, residues 1–91, of ribosomal protein TL5 from Thermus thermophilus binds specifically and strongly to the region of 5S rRNA containing loop E
G.M. Gongadze,Vladimir A. Meshcheryakov,Alexander Serganov,N.P. Fomenkova,Elena S. Mudrik,Bengt-Harald Jonsson,Anders Liljas,Stanislav Nikonov,Maria Garber +8 more
TL;DR: It is shown for the first time that the overproduced N‐terminal fragment (residues 1–91) of ribosomal protein TL5 binds specifically to 5S rRNA and that the region of this fragment containing residues 80–91 is a necessity for its RNA‐binding activity.