Evidence map›Paper›PMID 25846411›Full record

ArticleProteins2015

Crystal structure of a novel two domain GH78 family α-rhamnosidase from Klebsiella oxytoca with rhamnose bound.

Ellis C O'Neill, Clare E M Stevenson, Michael J Paterson, Martin Rejzek, Anne-Laure Chauvin, David M Lawson, Robert A Field

Open access · hybridAbstract read
In one paragraph

Article in Proteins, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
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  8. α-L-rhamnosidase: production, properties, and applications.World journal of microbiology & biotechnology · 2023
    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 2 countries.

Ellis C O'NeillDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich, Nr4 7UH, United Kingdom.
Clare E M StevensonDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich, Nr4 7UH, United Kingdom.
Michael J PatersonDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich, Nr4 7UH, United Kingdom.
Martin RejzekDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich, Nr4 7UH, United Kingdom.
Anne-Laure ChauvinLaboratorio Nacional De Genómica Para La Biodiversidad (Langebio), CINVESTAV-IPN, Irapuato, Cp36821, México.
David M LawsonDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich, Nr4 7UH, United Kingdom.
Robert A FieldDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich, Nr4 7UH, United Kingdom.
Norwich Research Park · GBJohn Innes Centre · GBCenter for Research and Advanced Studies of the National Polytechnic Institute · MX

Funding

Biotechnology and Biological Sciences Research Council BB/J004561/1Biotechnology and Biological Sciences Research Council BBS/E/J/000C0618
6 · The paper itself

Abstract

The crystal structure of the GH78 family α-rhamnosidase from Klebsiella oxytoca (KoRha) has been determined at 2.7 Å resolution with rhamnose bound in the active site of the catalytic domain. Curiously, the putative catalytic acid, Asp 222, is preceded by an unusual non-proline cis-peptide bond which helps to project the carboxyl group into the active centre. This KoRha homodimeric structure is significantly smaller than those of the other previously determined GH78 structures. Nevertheless, the enzyme displays α-rhamnosidase activity when assayed in vitro, suggesting that the additional structural domains found in the related enzymes are dispensible for function.

Indexed as

Protein Structure, TertiaryAmino Acid SequenceBacterial ProteinsBinding SitesBiocatalysisCarbohydrate ConformationCrystallography, X-RayGlycoside HydrolasesHydrogen-Ion ConcentrationKlebsiella oxytocaModels, MolecularMolecular Sequence DataProtein BindingRhamnoseSequence Homology, Amino AcidSubstrate Specificityalpha-L-rhamnosidaseBacterial ProteinsGlycoside HydrolasesRhamnoseE.C. 3.2.1.40enzyme structureflavonoidglycosyl hydrolase family 78rutinα-l-rhamnosidase

Identifiers

PMID25846411
PMCPMC4690510
OpenAlexW2126754039

What OpenQuestion holds

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LicenceCC BY
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.