Evidence map›Paper›PMID 18502766›Full record

ArticleThe Journal of biological chemistry2008

Structure and mechanism of the rebeccamycin sugar 4'-O-methyltransferase RebM.

Shanteri Singh, Jason G McCoy, Changsheng Zhang, Craig A Bingman, George N Phillips, Jon S Thorson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

32 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
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  5. ACS chemical biology · 2022
    Article
  6. Homology Modeling,Frontiers in cellular and infection microbiology · 2022
    Article
  7. Review
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  10. Review
  11. Article
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  15. Article
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  17. Characterization of the calicheamicin orsellinate C2-O-methyltransferase CalO6.Chembiochem : a European journal of chemical biology · 2014
    Article
  18. Article
  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

6 authors at 1 institution in 1 country.

Shanteri SinghDivision of Pharmaceutical Sciences, School of Pharmacy, University of Wisconsin, Madison, Wisconsin 53705, USA.
Jason G McCoy
Changsheng Zhang
Craig A Bingman
George N Phillips
Jon S Thorson
University of Wisconsin–Madison · US

Funding

Zeeh Pharmaceutical Experimental StationU19CA113297 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI SHEN, BEN · 2005 to 2009
$5.4M
In Vitro Glycorandomization of Natural ProductsR01AI052218 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI THORSON, JON SCOTT · 2002 to 2011
$3.8M
STUDIES ON CALICHEAMICIN BIOSYNTHESIS AND SELF RESISTANCER01CA084374 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI THORSON, JON SCOTT · 2000 to 2013
$3.6M
NCI NIH HHS CA84374NCI NIH HHS U19 CA113297NIAID NIH HHS AI52218
6 · The paper itself

Abstract

The 2.65-angstroms crystal structure of the rebeccamycin 4'-O-methyltransferase RebM in complex with S-adenosyl-l-homocysteine revealed RebM to adopt a typical S-adenosylmethionine-binding fold of small molecule O-methyltransferases (O-MTases) and display a weak dimerization domain unique to MTases. Using this structure as a basis, the RebM substrate binding model implicated a predominance of nonspecific hydrophobic interactions consistent with the reported ability of RebM to methylate a wide range of indolocarbazole surrogates. This model also illuminated the three putative RebM catalytic residues (His140/141 and Asp166) subsequently found to be highly conserved among sequence-related natural product O-MTases from GC-rich bacteria. Interrogation of these residues via site-directed mutagenesis in RebM demonstrated His140 and Asp166 to be most important for catalysis. This study reveals RebM to be a member of the general acid/base-dependent O-MTases and, as the first crystal structure for a sugar O-MTase, may also present a template toward the future engineering of natural product MTases for combinatorial applications.

Indexed as

CarbazolesCrystallizationCrystallography, X-RayEscherichia coliMethyltransferasesModels, MolecularMolecular ConformationProtein ConformationRecombinant ProteinsS-AdenosylhomocysteineStaurosporineCarbazolesMethyltransferasesrebeccamycinrebeccamycin 4'-O-methyltransferase, Lechevalieria aerocolonigenesRecombinant ProteinsS-AdenosylhomocysteineStaurosporine

Identifiers

PMID18502766
PMCPMC2504894
OpenAlexW2058345015

What OpenQuestion holds

Textmetadata
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.