Evidence map›Paper›PMID 17046787›Full record

ArticleJournal of molecular biology2007

RmlC, a C3' and C5' carbohydrate epimerase, appears to operate via an intermediate with an unusual twist boat conformation.

Changjiang Dong, Louise L Major, Velupillai Srikannathasan, James C Errey, Marie-France Giraud, Joseph S Lam, Michael Graninger, Paul Messner, Michael R McNeil, Robert A Field and 2 more

Abstract read
In one paragraph

Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 71 citations in OpenAlex.

  1. Dysregulation of a nucleotidyltransferase induces division and surface glycan defects inProceedings of the National Academy of Sciences of the United States of America · 2026
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  5. Review
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  7. Biosynthesis of d-Biochemistry · 2021
    Article
  8. Article
  9. Discovery of an RmlC/D fusion protein in the microalgaThe Journal of biological chemistry · 2019
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  11. Article
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  14. Review
  15. Article
  16. Biochemical studies on WbcA, a sugar epimerase from Yersinia enterocolitica.Protein science : a publication of the Protein Society · 2015
    Article
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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

12 authors at 3 institutions in 2 countries.

Changjiang DongCentre for Biomolecular Sciences, The University, St. Andrews KY16 9ST, UK.
Louise L Major
Velupillai Srikannathasan
James C Errey
Marie-France Giraud
Joseph S Lam
Michael Graninger
Paul Messner
Michael R McNeil
Robert A Field
Chris Whitfield
James H Naismith
University of St Andrews · GBUniversity of East Anglia · GBColorado State University · US

Funding

Structure of enzymes in Multi-Drug Resistant Tuberculosis (MDR-TB)P01AI057836 · NIAID · COLORADO STATE UNIVERSITY-FORT COLLINS · PI MCNEIL, MICHAEL R · 2004 to 2008
$4.5M
Austrian Science Fund FWF P 18013Biotechnology and Biological Sciences Research Council BBS/E/J/000C0618NIAID NIH HHS P01 AI057836Wellcome Trust 067305Wellcome Trust 081862
6 · The paper itself

Abstract

The striking feature of carbohydrates is their constitutional, conformational and configurational diversity. Biology has harnessed this diversity and manipulates carbohydrate residues in a variety of ways, one of which is epimerization. RmlC catalyzes the epimerization of the C3' and C5' positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. RmlC is the third enzyme of the rhamnose pathway, and represents a validated anti-bacterial drug target. Although several structures of the enzyme have been reported, the mechanism and the nature of the intermediates have remained obscure. Despite its relatively small size (22 kDa), RmlC catalyzes four stereospecific proton transfers and the substrate undergoes a major conformational change during the course of the transformation. Here we report the structure of RmlC from several organisms in complex with product and product mimics. We have probed site-directed mutants by assay and by deuterium exchange. The combination of structural and biochemical data has allowed us to assign key residues and identify the conformation of the carbohydrate during turnover. Clear knowledge of the chemical structure of RmlC reaction intermediates may offer new opportunities for rational drug design.

Indexed as

Bacterial ProteinsCarbohydrate ConformationCarbohydrate DehydrogenasesCarbohydrate EpimerasesCrystallography, X-RayModels, MolecularNucleoside Diphosphate SugarsPseudomonas aeruginosaRecombinant ProteinsRhamnoseThymine NucleotidesBacterial ProteinsCarbohydrate DehydrogenasesCarbohydrate EpimerasesdTDP-4-ketorhamnose 3,5-epimeraseGDPmannose 3,5-epimeraseNucleoside Diphosphate SugarsRecombinant ProteinsRhamnosethymidine diphosphate-6-deoxy-xylo-4-hexuloseThymine Nucleotides

Identifiers

PMID17046787
PMCPMC1805628
OpenAlexW2116786068

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.