Evidence map›Paper›PMID 22413840›Full record

ArticleBiochemistry2012

Role of Gly117 in the cation/melibiose symport of MelB of Salmonella typhimurium.

Lan Guan, S Vivek Jakkula, Alexey A Hodkoff, Yue Su

Abstract read
In one paragraph

Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 22% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Allosteric effects of the coupling cation in melibiose transporter MelB.bioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. The proton electrochemical gradient induces a kinetic asymmetry in the symport cycle of LacY.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
  9. Article
  10. pKProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  11. Article
  12. Thermodynamic mechanism for inhibition of lactose permease by the phosphotransferase protein IIAGlc.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Lan GuanDepartment of Cell Physiology & Molecular Biophysics, Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, Texas 79430, USA. Lan.Guan@ttuhsc.edu
S Vivek Jakkula
Alexey A Hodkoff
Yue Su
Texas Tech University · USTexas Tech University Health Sciences Center · US

Funding

Novel capture reagents for membrane protein structure determinationR01GM095538 · NIGMS · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI GUAN, LAN · 2010 to 2013
$1.2M
Crystallization of eukaryotic facilitated glucose transportersR21HL087895 · NHLBI · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI GUAN, LAN · 2008 to 2009
$612k
NHLBI NIH HHS R21 HL087895NHLBI NIH HHS R21HL087895-02S1NIGMS NIH HHS R01 GM095538
6 · The paper itself

Abstract

The melibiose permease of Salmonella typhimurium (MelB(St)) catalyzes symport of melibiose with Na(+), Li(+), or H(+), and bioinformatics analysis indicates that a conserved Gly117 (helix IV) is part of the Na(+)-binding site. We mutated Gly117 to Ala, Pro, Trp, or Arg; the effects on melibiose transport and binding of cosubstrates depended on the physical-chemical properties of the side chain. Compared with WT MelB(St), the Gly117 → Ala mutant exhibited little difference in either cosubstrate binding or stimulation of melibiose transport by Na(+) or Li(+), but all other mutations reduced melibiose active transport and efflux, and decreased the apparent affinity for Na(+). The bulky Trp at position 117 caused the greatest inhibition of melibiose binding, and Gly117 → Arg yielded less than a 4-fold decrease in the apparent affinity for melibiose at saturating Na(+) or Li(+) concentration. Remarkably, the mutant Gly117 → Arg catalyzed melibiose exchange in the presence of Na(+) or Li(+), but did not catalyze melibiose translocation involving net flux of the coupling cation, indicating that sugar is released prior to release of the coupling cation. Taken together, the findings are consistent with the notion that Gly117 plays an important role in cation binding and translocation.

Indexed as

Bacterial ProteinsGlycineMelibioseModels, MolecularSalmonella typhimuriumBacterial ProteinsGlycineMelibiose

Identifiers

PMID22413840
PMCPMC3334291
OpenAlexW2161342689

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.