Evidence map›Paper›PMID 20876133›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Structural basis for the autoprocessing of zinc metalloproteases in the thermolysin family.

Xiang Gao, Jue Wang, Da-Qi Yu, Fei Bian, Bin-Bin Xie, Xiu-Lan Chen, Bai-Cheng Zhou, Lu-Hua Lai, Zhi-Xin Wang, Jia-Wei Wu and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

25 citing papers in PubMed, 56 citations in OpenAlex.

  1. A halophilic metalloprotease fromFrontiers in microbiology · 2025
    Article
  2. Article
  3. Protein sociology of ProA, Mip and other secreted virulence factors at theFrontiers in cellular and infection microbiology · 2023
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Biotechnology reports (Amsterdam, Netherlands) · 2018
    Article
  12. Article
  13. Article
  14. Article
  15. A novel mechanism of latency in matrix metalloproteinases.The Journal of biological chemistry · 2015
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Structure of gentlyase, the neutral metalloprotease of Paenibacillus polymyxa.Acta crystallographica. Section D, Biological crystallography · 2013
    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

11 authors at 3 institutions in 1 country.

Xiang GaoState Key Laboratory of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Jinan 250100, China.
Jue Wang
Da-Qi Yu
Fei Bian
Bin-Bin Xie
Xiu-Lan Chen
Bai-Cheng Zhou
Lu-Hua Lai
Zhi-Xin Wang
Jia-Wei Wu
Yu-Zhong Zhang
Shandong University · CNTsinghua University · CNPeking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thermolysin-like proteases (TLPs), a large group of zinc metalloproteases, are synthesized as inactive precursors. TLPs with a long propeptide (∼200 residues) undergo maturation following autoprocessing through an elusive molecular mechanism. We report the first two crystal structures for the autoprocessed complexes of a typical TLP, MCP-02. In the autoprocessed complex, Ala205 shifts upward by 33 Å from the previously covalently linked residue, His204, indicating that, following autocleavage of the peptide bond between His204 and Ala205, a large conformational change from the zymogen to the autoprocessed complex occurs. The eight N-terminal residues (residues Ala205-Gly212) of the catalytic domain form a new β-strand, nestling into two other β-strands. Simultaneously, the apparent T(m) of the autoprocessed complex increases 20 °C compared to that of the zymogen. The stepwise degradation of the propeptide begins with two sequential cuttings at Ser49-Val50 and Gly57-Leu58, which lead to the disassembly of the propeptide and the formation of mature MCP-02. Our findings give new insights into the molecular mechanism of TLP maturation.

Indexed as

Models, MolecularProtein ConformationChromatography, GelCircular DichroismCrystallizationElectrophoresis, Polyacrylamide GelEnzyme ActivationEnzyme PrecursorsMetalloendopeptidasesMutagenesis, Site-DirectedSequence Analysis, DNAEnzyme PrecursorsMetalloendopeptidases

Identifiers

PMID20876133
PMCPMC2955107
OpenAlexW1979576286

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.