pet44- rmtc Search Results


pet44-rmtc  (GenScript corporation)
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GenScript corporation pet44-rmtc
A . Secondary structure of the <t>E.</t> <t>coli</t> 16S rRNA, highlighting the modified nucleotide G1405 within h44 (purple), and other rRNA helices, h24 (green), h27 (yellow), and h45 (cyan), that comprise the conserved 16S rRNA surface recognized by RmtC. B . Postprocessed cryo-EM map of RmtC (red) bound to the 30S subunit with h44 (purple), body (dark gray) and head (white) domains indicated. C . Model of the 30S-RmtC complex, with RmtC and h44 shown as cartoon with a semi-transparent surface representation. D . RmtC (red semi-transparent surface) docks on the 30S subunit via interactions with helices h24, h27, h44, and h45 contacts made by both N-terminal subdomains (N1, dark red and N2, pink), and the C-terminal domain (white), including the Loop 237−246 region (teal). E and F , Two additional views of RmtC on the 16S rRNA surface.
Pet44 Rmtc, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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pet44-rmtc - by Bioz Stars, 2026-05
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Image Search Results


A . Secondary structure of the E. coli 16S rRNA, highlighting the modified nucleotide G1405 within h44 (purple), and other rRNA helices, h24 (green), h27 (yellow), and h45 (cyan), that comprise the conserved 16S rRNA surface recognized by RmtC. B . Postprocessed cryo-EM map of RmtC (red) bound to the 30S subunit with h44 (purple), body (dark gray) and head (white) domains indicated. C . Model of the 30S-RmtC complex, with RmtC and h44 shown as cartoon with a semi-transparent surface representation. D . RmtC (red semi-transparent surface) docks on the 30S subunit via interactions with helices h24, h27, h44, and h45 contacts made by both N-terminal subdomains (N1, dark red and N2, pink), and the C-terminal domain (white), including the Loop 237−246 region (teal). E and F , Two additional views of RmtC on the 16S rRNA surface.

Journal: bioRxiv

Article Title: 30S subunit recognition and G1405 modification by the aminoglycoside-resistance 16S ribosomal RNA methyltransferase RmtC

doi: 10.1101/2023.03.13.532395

Figure Lengend Snippet: A . Secondary structure of the E. coli 16S rRNA, highlighting the modified nucleotide G1405 within h44 (purple), and other rRNA helices, h24 (green), h27 (yellow), and h45 (cyan), that comprise the conserved 16S rRNA surface recognized by RmtC. B . Postprocessed cryo-EM map of RmtC (red) bound to the 30S subunit with h44 (purple), body (dark gray) and head (white) domains indicated. C . Model of the 30S-RmtC complex, with RmtC and h44 shown as cartoon with a semi-transparent surface representation. D . RmtC (red semi-transparent surface) docks on the 30S subunit via interactions with helices h24, h27, h44, and h45 contacts made by both N-terminal subdomains (N1, dark red and N2, pink), and the C-terminal domain (white), including the Loop 237−246 region (teal). E and F , Two additional views of RmtC on the 16S rRNA surface.

Article Snippet: RmtC (UniProt code Q33DX5) was expressed in E. coli using a modified pET44 plasmid encoding a synthetic E. coli codon-optimized gene (“pET44-RmtC”; GenScript) and subsequently purified by Ni 2+ -affinity and gel filtration chromatographies, as described previously ( ).

Techniques: Modification, Cryo-EM Sample Prep