Evidence map›Paper›PMID 10823940›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-A resolution.

D M van Aalten, B Synstad, M B Brurberg, E Hough, B W Riise, V G Eijsink, R K Wierenga

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

72 citing papers in PubMed, 268 citations in OpenAlex.

  1. Article
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  8. Article
  9. Genomic and Proteomic Study ofJournal of proteome research · 2021
    Article
  10. Plasmodium chitinases: revisiting a target of transmission-blockade against malaria.Protein science : a publication of the Protein Society · 2021
    Review
  11. Review
  12. AToxins · 2020
    Article
  13. Chitinases ofFrontiers in microbiology · 2019
    Review
  14. Review
  15. Review
  16. Article
  17. The deduced role of a chitinase containing two nonsynergistic catalytic domains.Acta crystallographica. Section D, Structural biology · 2018
    Article
  18. Structure, Catalysis, and Inhibition ofThe Journal of biological chemistry · 2017
    Article
  19. Article
  20. Article

12 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

D M van AaltenBiocenter Oulu, Department of Biochemistry, University of Oulu, Linnanmaa, FIN-90570 Oulu, Finland. dava@davapc1.bioch.dundee.ac.uk
B Synstad
M B Brurberg
E Hough
B W Riise
V G Eijsink
R K Wierenga
University of Oulu · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this paper, we describe the structure of chitinase B from Serratia marcescens, which consists of a catalytic domain with a TIM-barrel fold and a 49-residue C-terminal chitin-binding domain. This chitinase is the first structure of a bacterial exochitinase, and it represents one of only a few examples of a glycosyl hydrolase structure having interacting catalytic and substrate-binding domains. The chitin-binding domain has exposed aromatic residues that contribute to a 55-A long continuous aromatic stretch extending into the active site. Binding of chitin oligomers is blocked beyond the -3 subsite, which explains why the enzyme has chitotriosidase activity and degrades the chitin chain from the nonreducing end. Comparison of the chitinase B structure with that of chitinase A explains why these enzymes act synergistically in the degradation of chitin.

Indexed as

Crystallography, X-RayAcetylglucosamineAmino Acid SequenceBacterial ProteinsBinding SitesCatalytic DomainChitinChitinasesHexosaminidasesHydrogen BondingModels, MolecularMolecular Sequence DataMuramidasePlant ProteinsProtein ConformationProtein Structure, TertiaryAcetylglucosamineBacterial ProteinsChitinChitinaseschitotriosidasehevamineHexosaminidasesMuramidasePlant ProteinsPLC-B protein, Phytolacca americana

Identifiers

PMID10823940
PMCPMC18521
OpenAlexW2155082155

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.