Evidence map›Paper›PMID 20947023›Full record

ArticleStructure (London, England : 1993)2010

Structural insight into serine protease Rv3671c that Protects M. tuberculosis from oxidative and acidic stress.

Tapan Biswas, Jennifer Small, Omar Vandal, Toshiko Odaira, Haiteng Deng, Sabine Ehrt, Oleg V Tsodikov

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

25 citing papers in PubMed, 44 citations in OpenAlex.

  1. Cell wall remodeling-dependent morphotype switch inProceedings of the National Academy of Sciences of the United States of America · 2026
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  3. An unusual genetic switch controlsbioRxiv : the preprint server for biology · 2025
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  7. Review
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  12. The EMBO journal · 2017
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  14. Review
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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

7 authors at 3 institutions in 1 country.

Tapan BiswasDepartment of Medicinal Chemistry, College of Pharmacy, University of Michigan, Ann Arbor, MI 48109, USA.
Jennifer Small
Omar Vandal
Toshiko Odaira
Haiteng Deng
Sabine Ehrt
Oleg V Tsodikov
Cornell University · USUniversity of Michigan–Ann Arbor · USRockefeller University · US

Funding

pH Homeostasis in Mycobacterium tuberculosisR01AI081725 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI EHRT, SABINE · 2009 to 2013
$2.8M
NIAID NIH HHS R01 AI081725NIAID NIH HHS R0I AI081725
6 · The paper itself

Abstract

Rv3671c, a putative serine protease, is crucial for persistence of Mycobacterium tuberculosis in the hostile environment of the phagosome. We show that Rv3671c is required for M. tuberculosis resistance to oxidative stress in addition to its role in protection from acidification. Structural and biochemical analyses demonstrate that the periplasmic domain of Rv3671c is a functional serine protease of the chymotrypsin family and, remarkably, that its activity increases on oxidation. High-resolution crystal structures of this protease in an active strained state and in an inactive relaxed state reveal that a solvent-exposed disulfide bond controls the protease activity by constraining two distant regions of Rv3671c and stabilizing it in the catalytically active conformation. In vitro biochemical studies confirm that activation of the protease in an oxidative environment is dependent on this reversible disulfide bond. These results suggest that the disulfide bond modulates activity of Rv3671c depending on the oxidative environment in vivo.

Indexed as

Protein Structure, TertiaryBacterial ProteinsBinding SitesCrystallizationCysteineDisulfidesElectrophoresis, Polyacrylamide GelHydrogen-Ion ConcentrationModels, MolecularMutationMycobacterium tuberculosisOxidation-ReductionOxidative StressProtein BindingProtein ConformationProtein Structure, SecondaryBacterial ProteinsCysteineDisulfidesSerine Proteases

Identifiers

PMID20947023
PMCPMC2955984
OpenAlexW2054705564

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.