Evidence map›Paper›PMID 21847100›Full record

ArticleThe EMBO journal2011

Structural analysis of the Ras-like G protein MglA and its cognate GAP MglB and implications for bacterial polarity.

Mandy Miertzschke, Carolin Koerner, Ingrid R Vetter, Daniela Keilberg, Edina Hot, Simone Leonardy, Lotte Søgaard-Andersen, Alfred Wittinghofer

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

56 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
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  3. Structural basis ofbioRxiv : the preprint server for biology · 2026
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  5. In situ architecture of a nucleoid-associated biomolecular co-condensate that regulates bacterial cell division.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  19. The small GTPase MglA together with the TPR domain protein SgmX stimulates type IV pili formation inProceedings of the National Academy of Sciences of the United States of America · 2020
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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

8 authors at 3 institutions in 1 country.

Mandy MiertzschkeStructural Biology Group, Max-Planck-Institute for Molecular Physiology, Dortmund, Germany.
Carolin Koerner
Ingrid R Vetter
Daniela Keilberg
Edina Hot
Simone Leonardy
Lotte Søgaard-Andersen
Alfred Wittinghofer
Max Planck Institute for Terrestrial Microbiology · DEMax Planck Institute of Molecular Physiology · DEMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The bacterium Myxococcus xanthus uses a G protein cycle to dynamically regulate the leading/lagging pole polarity axis. The G protein MglA is regulated by its GTPase-activating protein (GAP) MglB, thus resembling Ras family proteins. Here, we show structurally and biochemically that MglA undergoes a dramatic, GDP-GTP-dependent conformational change involving a screw-type forward movement of the central β2-strand, never observed in any other G protein. This movement and complex formation with MglB repositions the conserved residues Arg53 and Gln82 into the active site. Residues required for catalysis are thus not provided by the GAP MglB, but by MglA itself. MglB is a Roadblock/LC7 protein and functions as a dimer to stimulate GTP hydrolysis in a 2:1 complex with MglA. In vivo analyses demonstrate that hydrolysis mutants abrogate Myxococcus' ability to regulate its polarity axis changing the reversal behaviour from stochastic to oscillatory and that both MglA GTPase activity and MglB GAP catalysis are essential for maintaining a proper polarity axis.

Indexed as

Amino Acid SequenceArginineBacterial ProteinsCatalysisCatalytic DomainCell PolarityGlutamineGuanosine TriphosphateHydrolysisMolecular Sequence DataMyxococcus xanthusProtein Conformationras ProteinsArginineBacterial ProteinsGlutamineGuanosine TriphosphateMglA protein, Myxococcus xanthusras Proteins

Identifiers

PMID21847100
PMCPMC3199381
OpenAlexW1935830624

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.