Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/25353
Share/Export:
logo share SHARE logo core CORE BASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Title

A new autocatalytic activation mechanism for cysteine proteases revealed by Prevotella intermedia interpain A

AuthorsMallorquí-Fernández, Noemí; Manandhar, Surya P.; Mallorquí-Fernández, Goretti; Usón, Isabel CSIC ORCID ; Wawrzonek, Katarzyna; Kantyka, Tomasz; Solà, Maria CSIC ORCID ; Thøgersen, Ida B.; Enghild, Jan J.; Potempa, Jan; Gomis-Rüth, F. Xavier CSIC ORCID
KeywordsPeriodontal disease
Prevotella intermedia
Bacterial periodontal pathogen
Issue Date1-Feb-2008
PublisherAmerican Society for Biochemistry and Molecular Biology
CitationJournal of Biological Chemistry 283(5): 2871–2882 (2008)
AbstractPrevotella intermedia is a major periodontopathogen contributing to human gingivitis and periodontitis. Such pathogens release proteases as virulence factors that cause deterrence of host defences and tissue destruction. A new cysteine protease from the cysteine-histidine-dyad class, interpain A, was studied in its zymogenic and its self-processed mature form. The latter consists of a bivalved moiety made up by two subdomains. In the structure of a catalytic cysteine-to-alanine zymogen variant, the right subdomain interacts with an unusual prodomain, thus contributing to latency. Unlike the catalytic cysteine residue, already in its competent conformation in the zymogen, the catalytic histidine is swung out from its active conformation and trapped in a cage shaped by a backing helix, a zymogenic hairpin and a latency flap in the zymogen. Dramatic rearrangement of up to 20Å of these elements triggered by a tryptophan switch occurs during activation and accounts for a new activation mechanism for proteolytic enzymes. These findings can be extrapolated to related potentially pathogenic cysteine proteases such as Streprococcus pyogenes SpeB and Porphyromonas gingivalis periodontain.
Description20 pages, 5 figures, 2 tables.-- PMID: 17993455 [PubMed].-- PMCID: PMC2772895.-- NIHMSID: NIHMS65935.-- Available online Nov 7, 2007.
Publisher version (URL)http://dx.doi.org/10.1074/jbc.M708481200
URIhttp://hdl.handle.net/10261/25353
DOI10.1074/jbc.M708481200
ISSN0021-9258
E-ISSN1083-351X
Appears in Collections:(IBMB) Artículos

Files in This Item:
File Description SizeFormat
Mallorqui_Fernandez_et_al.pdf4,23 MBAdobe PDFThumbnail
View/Open
Show full item record
Review this work

PubMed Central
Citations

25
checked on May 13, 2022

SCOPUSTM   
Citations

33
checked on May 14, 2022

WEB OF SCIENCETM
Citations

34
checked on May 16, 2022

Page view(s)

393
checked on May 18, 2022

Download(s)

250
checked on May 18, 2022

Google ScholarTM

Check

Altmetric

Dimensions


Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.