Evidence map›Paper›PMID 18171624›Full record

ArticleJournal of structural biology2008

Structures of open (R) and close (T) states of prephenate dehydratase (PDT)--implication of allosteric regulation by L-phenylalanine.

Kemin Tan, Hui Li, Rongguang Zhang, Minyi Gu, Shonda T Clancy, Andrzej Joachimiak

Abstract read
In one paragraph

Article in Journal of structural biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

19 citing papers in PubMed, 37 citations in OpenAlex.

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  15. X-ray structure of prephenate dehydratase from Streptococcus mutans.Journal of microbiology (Seoul, Korea) · 2014
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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

6 authors at 2 institutions in 1 country.

Kemin TanMidwest Center for Structural Genomics and Structural Biology Center, Biosciences Division, Building 202, Room A125 9700, S. Cass Avenue, Argonne National Laboratory, Argonne, IL 60439, USA.
Hui Li
Rongguang Zhang
Minyi Gu
Shonda T Clancy
Andrzej Joachimiak
Argonne National Laboratory · USJoint Center for Structural Genomics · US

Funding

The Midwest Center for Structural GenomicsU54GM074942 · NIGMS · UNIVERSITY OF CHICAGO · PI JOACHIMIAK, ANDRZEJ · 2005 to 2009
$51.0M
NIGMS NIH HHS GM074942NIGMS NIH HHS U54 GM074942
6 · The paper itself

Abstract

The enzyme prephenate dehydratase (PDT) converts prephenate to phenylpyruvate in L-phenylalanine biosynthesis. PDT is allosterically regulated by L-Phe and other amino acids. We report the first crystal structures of PDT from Staphylococcus aureus in a relaxed (R) state and PDT from Chlorobium tepidum in a tense (T) state. The two enzymes show low sequence identity (27.3%) but the same prototypic architecture and domain organization. Both enzymes are tetramers (dimer of dimers) in crystal and solution while a PDT dimer can be regarded as a basic catalytic unit. The N-terminal PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In one PDT dimer two clefts are aligned to form an extended active site across the dimer interface. Similarly at the interface two ACT regulatory domains create two highly conserved pockets. Upon binding of the L-Phe inside the pockets, PDT transits from an open to a closed conformation.

Indexed as

Allosteric RegulationAmino Acid SequenceBacterial ProteinsChlorobiumCrystallography, X-RayDimerizationModels, MolecularMolecular Sequence DataMolecular StructurePhenylalaninePrephenate DehydrataseProtein BindingProtein Structure, SecondaryProtein Structure, TertiarySequence Homology, Amino AcidStaphylococcus aureusBacterial ProteinsPhenylalaninePrephenate Dehydratase

Identifiers

PMID18171624
PMCPMC3366492
OpenAlexW2114660738

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.