Structure of mammalian plasma fetuin-B and its mechanism of selective metallopeptidase inhibition.
X-ray crystallography
enzyme mechanisms
mammalian fertilization
metallopeptidase
multi-protein complexes
polyspermy
protein inhibitor
protein structure
sperm–egg fusion
structure determination
Journal
IUCrJ
ISSN: 2052-2525
Titre abrégé: IUCrJ
Pays: England
ID NLM: 101623101
Informations de publication
Date de publication:
01 Mar 2019
01 Mar 2019
Historique:
received:
13
11
2018
accepted:
28
01
2019
entrez:
15
3
2019
pubmed:
15
3
2019
medline:
15
3
2019
Statut:
epublish
Résumé
Mammalian fetuin-A and fetuin-B are abundant serum proteins with pleiotropic functions. Fetuin-B is a highly selective and potent inhibitor of metallo-peptidases (MPs) of the astacin family, which includes ovastacin in mammals. By inhibiting ovastacin, fetuin-B is essential for female fertility. The crystal structure of fetuin-B was determined unbound and in complex with archetypal astacin, and it was found that the inhibitor has tandem cystatin-type modules (CY1 and CY2). They are connected by an exposed linker with a rigid, disulfide-linked 'CPDCP-trunk', and are followed by a C-terminal region (CTR) with little regular secondary structure. The CPDCP-trunk and a hairpin of CY2 form a bipartite wedge, which slots into the active-site cleft of the MP. These elements occupy the nonprimed and primed sides of the cleft, respectively, but spare the specificity pocket so that the inhibitor is not cleaved. The aspartate in the trunk blocks the catalytic zinc of astacin, while the CY2 hairpin binds through a QWV
Identifiants
pubmed: 30867929
doi: 10.1107/S2052252519001568
pii: jt5031
pmc: PMC6400186
doi:
Types de publication
Journal Article
Langues
eng
Pagination
317-330Références
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