Crystal structure of a type II dehydroquinate dehydratase-like protein from Bifidobacterium longum.

Samuel H Light, Sankar N Krishna, Raymond C Bergan, Arnon Lavie, Wayne F Anderson

Open access · greenAbstract read

In one paragraph

Article in Journal of structural and functional genomics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

0.2field-weighted citation impact, top 52% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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

5 authors at 3 institutions in 1 country.

Samuel H LightCenter for Structural Genomics of Infectious Diseases and Department of Molecular Pharmacology and Biological Chemistry, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.

Sankar N Krishna

Raymond C Bergan

Arnon Lavie

Wayne F Anderson

Northwestern University · USRobert H. Lurie Comprehensive Cancer Center of Northwestern UniversityUniversity of Illinois Chicago · US

Funding

NIAID NIH HHS HHSN272200700058CNIAID NIH HHS HHSN272201200026C

6 · The paper itself

Abstract

Dehydroquinate dehydratase (DHQD) catalyzes the third step in the biosynthetic shikimate pathway. Here we identify a Bifidobacterium longum protein with high sequence homology to type II DHQDs but no detectable DHQD activity under standard assay conditions. A crystal structure reveals that the B. longum protein adopts a DHQD-like tertiary structure but a distinct quaternary state. Apparently forming a dimer, the B. longum protein lacks the active site aspartic acid contributed from a neighboring protomer in the type II DHQD dodecamer. Relating to the absence of protein-protein interactions established in the type II DHQD dodecameric assembly, substantial conformational changes distinguish the would-be active site of the B. longum protein. As B. longum possess no other genes with homology to known DHQDs, these findings imply a unique DHQD activity within B. longum.

Indexed as

Models, MolecularAmino Acid SequenceBacterial ProteinsBifidobacteriumCrystallography, X-RayEscherichia coliHydro-LyasesMolecular Sequence DataProtein MultimerizationProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsSequence Homology, Amino AcidShikimic Acid3-dehydroquinate dehydrataseBacterial ProteinsHydro-LyasesRecombinant ProteinsShikimic Acid

Identifiers

PMID23539270

DOI10.1007/s10969-013-9149-7

PMCPMC3878977

OpenAlexW2015032580

What OpenQuestion holds

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Registered trials

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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.