ArticleBiochemistry2005
Importance of the GP dipeptide of the antiporter motif and other membrane-embedded proline and glycine residues in tetracycline efflux protein Tet(L).
Article in Biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Inhibition of Multidrug Efflux Pumps Belonging to the Major Facilitator Superfamily in Bacterial Pathogens.Biomedicines · 2023Review
- The Major Facilitator Superfamily and Antimicrobial Resistance Efflux Pumps of the ESKAPEE PathogenAntibiotics (Basel, Switzerland) · 2023Review
- Evidence of pediatric sepsis caused by a drug resistantEmerging microbes & infections · 2022Article
- Mutagenesis and functional analysis of SotB: A multidrug transporter of the major facilitator superfamily fromFrontiers in microbiology · 2022Article
- Structures and General Transport Mechanisms by the Major Facilitator Superfamily (MFS).Chemical reviews · 2021Article
- Staphylococcus aureus Tet38 Efflux Pump Structural Modeling and Roles of Essential Residues in Drug Efflux and Host Cell Internalization.Infection and immunity · 2021Article
- Functional and Structural Roles of the Major Facilitator Superfamily Bacterial Multidrug Efflux Pumps.Microorganisms · 2020Review
- Crystal structures of MdfA complexed with acetylcholine and inhibitor reserpine.Biophysics reports · 2016Article
- Substrate-bound structure of the E. coli multidrug resistance transporter MdfA.Cell research · 2015Article
- Multidrug efflux pumps from Enterobacteriaceae, Vibrio cholerae and Staphylococcus aureus bacterial food pathogens.International journal of environmental research and public health · 2015Review
- Bacillus cereus efflux protein BC3310 - a multidrug transporter of the unknown major facilitator family, UMF-2.Frontiers in microbiology · 2015Article
- Biochemistry of bacterial multidrug efflux pumps.International journal of molecular sciences · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Proline and glycine residues are well represented among functionally important residues in hydrophobic domains of membrane transport proteins, and several critical roles have been suggested for them. Here, the effects of mutational changes in membrane-embedded proline and glycine residues of Tet(L) were examined, with a focus on the conserved GP(155,156) dipeptide of motif C, a putative "antiporter motif". Mutation of Gly155 to cysteine resulted in a mutant Tet(L) that bound its tetracycline-divalent metal (Tc-Me2+) substrate but did not catalyze efflux or exchange of Tc-Me2+ or catalyze uptake or exchange of Rb+ which was used to monitor the coupling ion. These results support suggestions that this region is involved in the conformational changes required for translocation. Mutations in Pro156 resulted in reduction (P156G) or loss (P156A or P156C) of Tc-Me2+ efflux capacity. All three Pro156 mutants exhibited a K+ leak (monitored by 86Rb+ fluxes) that was not observed in wild-type Tet(L). A similar leak was observed in a mutant in a membrane-embedded proline residue elsewhere in the Tet(L) protein (P175C) as well as in a P156C mutant of related antiporter Tet(K). These findings are consistent with roles proposed for membrane-embedded prolines in tight helix packing. Patterns of Tc resistance conferred by additional Tet(L) mutants indicate important roles for another GP dipeptide in transmembrane segment (TMS) X as well as for membrane-embedded glycine residues in TMS XIII.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.