Evidence map›Paper›PMID 11045630›Full record

ArticleProtein science : a publication of the Protein Society2000

Structure of streptococcal pyrogenic exotoxin A reveals a novel metal cluster.

C A Earhart, G M Vath, M Roggiani, P M Schlievert, D H Ohlendorf

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

13 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Nasopharyngeal infection byProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Crystal structure of a dimeric form of streptococcal pyrogenic exotoxin A (SpeA1).Protein science : a publication of the Protein Society · 2004
    Article
  10. Article
  11. Article
  12. Review
  13. 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

5 authors at 2 institutions in 1 country.

C A EarhartDepartment of Biochemistry, University of Minnesota Medical School, Minneapolis 55455, USA.
G M Vath
M Roggiani
P M Schlievert
D H Ohlendorf
University of Minnesota Medical Center · USUniversity of Minnesota · US

Funding

CARDIOTOXICITY OF STREPTOCOCCAL PYROGENIC EXOTOXINSR01HL036611 · NHLBI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI SCHLIEVERT, PATRICK M · 1986 to 2006
$1.3M
MOLECULAR BIOPHYSICS TRAINING PROGRAMT32GM008277 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID DALE · 1988 to 2002
$696k
STRUCTURAL STUDIES OF SUPERANTIGENSR01GM054384 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI OHLENDORF, DOUGLAS H · 1996 to 1999
–
CARDIOTOXICITY OF STREPTOCOCCAL PYROGENIC EXOTOXINR55HL036611 · NHLBI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI SCHLIEVERT, PATRICK M · 1992 to 1992
–
NHLBI NIH HHS HL-36611NIGMS NIH HHS GM 08277NIGMS NIH HHS GM-54384
6 · The paper itself

Abstract

The streptococcal pyrogenic toxins A, B, and C (SPEA, SPEB, and SPEC) are responsible for the fever, rash, and other toxicities associated with scarlet fever and streptococcal toxic shock syndrome. This role, together with the ubiquity of diseases caused by Streptococcus pyogenes, have prompted structural analyses of SPEA by several groups. Papageorgiou et al. (1999) have recently reported the structure of SPEA crystallized in the absence of zinc. Zinc has been shown to be important in the ability of some staphylococcal and streptococcal toxins to stimulate proliferation of CD4+ T-cells. Since cadmium is more electron dense than zinc and typically binds interchangeably, we grew crystals in the presence of 10 mM CdCl2. Crystals have been obtained in three space groups, and the structure in the P2(1)2(1)2(1) crystal form has been refined to 1.9 A resolution. The structural analysis revealed an identical tetramer as well as a novel tetrahedral cluster of cadmium in all three crystal forms on a disulfide loop encompassing residues 87-98. No cadmium was bound at the site homologous to the zinc site in staphylococcal enterotoxins C (SECs) despite the high structural homology between SPEA and SECs. Subsequent soaking of crystals grown in the presence of cadmium in 10 mM ZnCl2 showed that zinc binds in this site (indicating it can discriminate between zinc and cadmium ions) using the three ligands (Asp77, His106, and His110) homologous to the SECs plus a fourth ligand (Glu33).

Indexed as

Bacterial ProteinsMembrane ProteinsExotoxinsMetalsModels, MolecularProtein ConformationBacterial Proteinserythrogenic toxinExotoxinsMembrane ProteinsMetalsSpeA protein, Streptococcus pyogenes

Identifiers

PMID11045630
PMCPMC2144691
OpenAlexW2170835076

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.