Evidence map›Paper›PMID 21471968›Full record

ArticleNature2011

Crystal structure of a phosphorylation-coupled saccharide transporter.

Yu Cao, Xiangshu Jin, Elena J Levin, Hua Huang, Yinong Zong, Matthias Quick, Jun Weng, Yaping Pan, James Love, Marco Punta and 5 more

Abstract read
In one paragraph

Article in Nature, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
–field-weighted citation impact
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

37 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Crystal structure of the NaNature communications · 2022
    Article
  5. Article
  6. Article
  7. Harnessing a Transient Gene Expression System inPlants (Basel, Switzerland) · 2021
    Article
  8. Transporters of glucose and other carbohydrates in bacteria.Pflugers Archiv : European journal of physiology · 2020
    Review
  9. Elevator-type mechanisms of membrane transport.Biochemical Society transactions · 2020
    Review
  10. Article
  11. Article
  12. Article
  13. Structure of an EIIC sugar transporter trapped in an inward-facing conformation.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

15 authors.

Yu CaoDepartment of Physiology & Cellular Biophysics, College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, New York 10032, USA.
Xiangshu Jin
Elena J Levin
Hua Huang
Yinong Zong
Matthias Quick
Jun Weng
Yaping Pan
James Love
Marco Punta
Burkhard Rost
Wayne A Hendrickson
Jonathan A Javitch
Kanagalaghatta R Rajashankar
Ming Zhou

Funding

Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
Structural mechanism of K channel modulation by cellular redox stateR01HL086392 · NHLBI · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI ZHOU, MING · 2006 to 2018
$3.9M
Multidisciplinary Training in Translational Cardiovascular ResearchT32HL087745 · NHLBI · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI MARKS, ANDREW ROBERT · 2007 to 2011
$1.8M
Structure and function of urea transportersR01DK088057 · NIDDK · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI ZHOU, MING · 2010 to 2014
$1.7M
Molecular Determinants for the Action of PsychostimulantsK05DA022413 · NIDA · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI JAVITCH, JONATHAN A · 2007 to 2016
$1.3M
Structure and Function of a Phosphorylation Coupled Saccharide TransporterR01GM098878 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI ZHOU, MING · 2011 to 2014
$1.2M
NHLBI NIH HHS R01 HL086392NHLBI NIH HHS T32HL087745NIBIB NIH HHS P30 EB009998NIDA NIH HHS K05 DA022413NIDDK NIH HHS DK088057NIDDK NIH HHS R01 DK088057NIGMS NIH HHS GM05026NIGMS NIH HHS GM05026-SUB0007NIGMS NIH HHS GM098878NIGMS NIH HHS R01 GM098878
6 · The paper itself

Abstract

Saccharides have a central role in the nutrition of all living organisms. Whereas several saccharide uptake systems are shared between the different phylogenetic kingdoms, the phosphoenolpyruvate-dependent phosphotransferase system exists almost exclusively in bacteria. This multi-component system includes an integral membrane protein EIIC that transports saccharides and assists in their phosphorylation. Here we present the crystal structure of an EIIC from Bacillus cereus that transports diacetylchitobiose. The EIIC is a homodimer, with an expansive interface formed between the amino-terminal halves of the two protomers. The carboxy-terminal half of each protomer has a large binding pocket that contains a diacetylchitobiose, which is occluded from both sides of the membrane with its site of phosphorylation near the conserved His250 and Glu334 residues. The structure shows the architecture of this important class of transporters, identifies the determinants of substrate binding and phosphorylation, and provides a framework for understanding the mechanism of sugar translocation.

Indexed as

Models, MolecularBacillus cereusBinding SitesCarbohydrate MetabolismCrystallizationMembrane Transport ProteinsPhosphorylationProtein Structure, QuaternaryProtein Structure, TertiaryMembrane Transport Proteins

Identifiers

PMID21471968
PMCPMC3201810

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Registered trials

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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.