Evidence map›Paper›PMID 23526584›Full record

ArticleProteins2013

Crystal structure of SsfS6, the putative C-glycosyltransferase involved in SF2575 biosynthesis.

Fengbin Wang, Maoquan Zhou, Shanteri Singh, Ragothaman M Yennamalli, Craig A Bingman, Jon S Thorson, George N Phillips

Abstract read
In one paragraph

Article in Proteins, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

12 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Article
  3. Exploring the catalytic function and active sites of a novelSynthetic and systems biotechnology · 2022
    Article
  4. OleD Loki as a Catalyst for Hydroxamate Glycosylation.Chembiochem : a European journal of chemical biology · 2020
    Article
  5. Article
  6. OleD Loki as a Catalyst for Tertiary Amine and Hydroxamate Glycosylation.Chembiochem : a European journal of chemical biology · 2017
    Article
  7. Enzymatic synthesis of glycosides: from naturalBeilstein journal of organic chemistry · 2017
    Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. 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

7 authors at 3 institutions in 1 country.

Fengbin WangDepartment of Biochemistry and Cell Biology, Rice University, Houston, Texas 77005, USA.
Maoquan Zhou
Shanteri Singh
Ragothaman M Yennamalli
Craig A Bingman
Jon S Thorson
George N Phillips
Rice University · USUniversity of Wisconsin–Madison · USUniversity of Kentucky · US

Funding

In Vitro Glycorandomization of Natural ProductsR37AI052218 · NIAID · UNIVERSITY OF KENTUCKY · PI THORSON, JON SCOTT · 2012 to 2021
$4.0M
In Vitro Glycorandomization of Natural ProductsR01AI052218 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI THORSON, JON SCOTT · 2002 to 2011
$3.8M
Enzyme Discovery for Natural Product BiosynthesisU01GM098248 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI PHILLIPS, GEORGE NEAL · 2011 to 2015
$2.8M
NIAID NIH HHS AI52218NIAID NIH HHS R01 AI052218NIAID NIH HHS R37 AI052218NIGMS NIH HHS U01 GM098248NIGMS NIH HHS U01GM098248
6 · The paper itself

Abstract

The molecule known as SF2575 from Streptomyces sp. is a tetracycline polyketide natural product that displays antitumor activity against murine leukemia P388 in vivo. In the SF2575 biosynthetic pathway, SsfS6 has been implicated as the crucial C-glycosyltransferase (C-GT) that forms the C-C glycosidic bond between the sugar and the SF2575 tetracycline-like scaffold. Here, we report the crystal structure of SsfS6 in the free form and in complex with TDP, both at 2.4 Å resolution. The structures reveal SsfS6 to adopt a GT-B fold wherein the TDP and docked putative aglycon are consistent with the overall C-glycosylation reaction. As one of only a few existing structures for C-glycosyltransferases, the structures described herein may serve as a guide to better understand and engineer C-glycosylation.

Indexed as

Crystallography, X-RayAnimalsAnti-Bacterial AgentsBacterial ProteinsGlycosylationGlycosyltransferasesLeukemia P388MiceStreptomycesTetracyclinesAnti-Bacterial AgentsBacterial ProteinsGlycosyltransferasesSF 2575Tetracyclines

Identifiers

PMID23526584
PMCPMC3896073
OpenAlexW2102651786

What OpenQuestion holds

Textmetadata
LicenceTDM
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.