Evidence map›Paper›PMID 26524494›Full record

ArticleNature structural & molecular biology2015

Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase.

Laurent Cappadocia, Andrea Pichler, Christopher D Lima

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed, 1 pooled it
4.8field-weighted citation impact, top 4% 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

90 citing papers in PubMed, 1 synthesis or guideline pooled it, 139 citations in OpenAlex.

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30 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 2 countries.

Laurent CappadociaStructural Biology Program, Sloan Kettering Institute, New York, New York, USA.
Andrea PichlerDepartment of Epigenetics, Max Planck Institute of Immunobiology and Epigenetics, Freiburg, Germany.
Christopher D LimaStructural Biology Program, Sloan Kettering Institute, New York, New York, USA.
Kettering University · USMax Planck Institute of Immunobiology and Epigenetics · DE

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
X-RAY STRUCTURE OF RIFM PROTEIN FROM THE BIOSYNTHESIS PATHWAY OF THE ANSAMYCIN AP41RR012408 · NCRR · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI ORVILLE, ALLEN M · 1998 to 2011
$32.2M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
Structural studies of ubiquitin-like protein modificationR01GM065872 · NIGMS · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI LIMA, CHRISTOPHER D. · 2002 to 2015
$4.9M
Macromolecular Crystallography at the National Synchrotron Light SourceP41GM103473 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI SWEET, ROBERT M · 2012 to 2013
$4.9M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
Howard Hughes Medical InstituteNCI NIH HHS P30 CA008748NCRR NIH HHS P41 RR012408NCRR NIH HHS P41RR012408NCRR NIH HHS S10 RR029205NIBIB NIH HHS P30 EB009998NIGMS NIH HHS GM065872NIGMS NIH HHS P41 GM103403NIGMS NIH HHS P41 GM103473NIGMS NIH HHS P41GM103473NIGMS NIH HHS R01 GM065872
6 · The paper itself

Abstract

E3 protein ligases enhance transfer of ubiquitin-like (Ubl) proteins from E2 conjugating enzymes to substrates by stabilizing the thioester-charged E2~Ubl in a closed configuration optimally aligned for nucleophilic attack. Here, we report biochemical and structural data that define the N-terminal domain of the Homo sapiens ZNF451 as the catalytic module for SUMO E3 ligase activity. The ZNF451 catalytic module contains tandem SUMO-interaction motifs (SIMs) bridged by a Pro-Leu-Arg-Pro (PLRP) motif. The first SIM and PLRP motif engage thioester-charged E2~SUMO while the next SIM binds a second molecule of SUMO bound to the back side of E2. We show that ZNF451 is SUMO2 specific and that SUMO modification of ZNF451 may contribute to activity by providing a second molecule of SUMO that interacts with E2. Our results are consistent with ZNF451 functioning as a bona fide SUMO E3 ligase.

Indexed as

Amino Acid MotifsAminoacyltransferasesBinding SitesCrystallography, X-RayHumansProtein BindingProtein ConformationSUMO-1 ProteinTranscription FactorsUbiquitin-Protein LigasesAminoacyltransferasesSUMO-1 ProteinTranscription FactorsUbiquitin-Protein LigasesZNF451 protein, human

Identifiers

PMID26524494
PMCPMC4709122
OpenAlexW2245906427

What OpenQuestion holds

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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.