Evidence map›Paper›PMID 19233924›Full record

ArticleJournal of bacteriology2009

Structural insights into the extracytoplasmic thiamine-binding lipoprotein p37 of Mycoplasma hyorhinis.

Katherine H Sippel, Arthur H Robbins, Robbie Reutzel, Susan K Boehlein, Kazunori Namiki, Steve Goodison, Mavis Agbandje-McKenna, Charles J Rosser, Robert McKenna

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Improved transformation efficiency inMicrobiology spectrum · 2023
    Article
  2. Article
  3. Article
  4. A p37-based ELISA used to monitor anti- Mycoplasma hyorhinis IgG in serum from pigs immunized with inactivated M. hyorhinis vaccines.Journal of veterinary diagnostic investigation : official publication of the American Association of Veterinary Laboratory Diagnosticians, Inc · 2018
    Article
  5. Article
  6. Article
  7. Article
  8. Structure of a eukaryotic thiaminase I.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Cloning, expression, purification, crystallization and preliminary X-ray analysis of Mycoplasma genitalium protein MG289.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009
    Article
  15. Article
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

9 authors at 2 institutions in 1 country.

Katherine H SippelDepartment of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, FL 32610, USA.
Arthur H Robbins
Robbie Reutzel
Susan K Boehlein
Kazunori Namiki
Steve Goodison
Mavis Agbandje-McKenna
Charles J Rosser
Robert McKenna
University of Florida · USUniversity of Florida Health Science Center · US

Funding

ZINC FINGER-DNA COMPLEXP41RR001646 · NCRR · CORNELL UNIVERSITY ITHACA · PI CINGOLANI, GINO · 1985 to 2011
$23.8M
NCRR NIH HHS P41 RR001646NCRR NIH HHS RR001646NIGMS NIH HHS DMR-0225180
6 · The paper itself

Abstract

The Mycoplasma hyorhinis protein p37 has been implicated in tumorigenic transformation for more than 20 years. Though there are many speculations as to its function, based solely on sequence homology, the issue has remained unresolved. Presented here is the 1.6-A-resolution refined crystal structure of M. hyorhinis p37, renamed the extracytoplasmic thiamine-binding lipoprotein (Cypl). The structure shows thiamine pyrophosphate (TPP) and two calcium ions are bound to Cypl and give the first insights into possible functions of the Cypl-like family of proteins. Sequence alignments of Cypl-like proteins between several different species of mycoplasma show that the thiamine-binding site is likely conserved and structural alignments reveal the similarity of Cypl to various binding proteins. While the experimentally determined function of Cypl remains unknown, the structure shows that the protein is a TPP-binding protein, opening up many avenues for future mechanistic studies and making Cypl a possible target for combating mycoplasma infections and tumorigenic transformation.

Indexed as

Bacterial ProteinsBinding SitesCalciumCarrier ProteinsCations, DivalentConserved SequenceCrystallography, X-RayLipoproteinsModels, MolecularMycoplasma hyorhinisProtein Structure, TertiaryThiamine PyrophosphateBacterial ProteinsCalciumCarrier ProteinsCations, DivalentLipoproteinsthiamine-binding proteinThiamine Pyrophosphate

Identifiers

PMID19233924
PMCPMC2668404
OpenAlexW2152258739

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.