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
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

317-330

Références

Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2256-68
pubmed: 15572779
J Mol Evol. 1990 Jan;30(1):60-71
pubmed: 2107324
FEBS Lett. 1993 Sep 27;331(1-2):134-40
pubmed: 8405391
J Phys Colloid Chem. 1947 Jan;51(1):164-71
pubmed: 20286396
Biochim Biophys Acta. 2012 Jan;1824(1):157-63
pubmed: 21558023
Angew Chem Int Ed Engl. 2011 Oct 24;50(44):10357-60
pubmed: 21915964
Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):125-32
pubmed: 20124692
Circ Res. 2011 Jun 10;108(12):1494-509
pubmed: 21659653
Proc Natl Acad Sci U S A. 2012 Oct 2;109(40):16131-6
pubmed: 22988105
Nat Struct Biol. 2003 Dec;10(12):980
pubmed: 14634627
FEBS Lett. 1991 Jul 22;285(2):213-9
pubmed: 1855589
Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):235-42
pubmed: 21460441
Protein Sci. 2014 Feb;23(2):123-44
pubmed: 24596965
J Mol Biol. 2008 Dec 5;384(1):228-39
pubmed: 18824173
Acta Crystallogr D Biol Crystallogr. 2006 Oct;62(Pt 10):1243-50
pubmed: 17001101
Nat Struct Mol Biol. 2015 Nov;22(11):833-4
pubmed: 26581513
J Comput Chem. 2004 Oct;25(13):1605-12
pubmed: 15264254
Dev Cell. 2013 Apr 15;25(1):106-12
pubmed: 23562279
J Struct Biol. 2016 Apr;194(1):1-7
pubmed: 26850170
Curr Protoc Protein Sci. 2016 Feb 02;83:21.16.1-21.16.20
pubmed: 26836407
J Mol Biol. 1993 Dec 20;234(4):1060-9
pubmed: 8263913
Biochem J. 2003 Nov 15;376(Pt 1):135-45
pubmed: 12943536
Biochim Biophys Acta. 1969;185(2):269-86
pubmed: 4980133
J Biol Chem. 2009 Jun 5;284(23):15353-7
pubmed: 19201757
Cell. 2006 Jan 13;124(1):147-59
pubmed: 16413488
Front Biosci (Landmark Ed). 2009 Jan 01;14(8):2911-22
pubmed: 19273244
Crit Rev Biochem Mol Biol. 2008 Sep-Oct;43(5):319-45
pubmed: 18937105
Acta Crystallogr D Struct Biol. 2018 Feb 1;74(Pt 2):143-151
pubmed: 29533240
Biochem J. 2000 Sep 1;350 Pt 2:589-97
pubmed: 10947975
Angew Chem Int Ed Engl. 2015 Mar 2;54(10):2917-21
pubmed: 25630877
J Biol Chem. 2010 Apr 30;285(18):13958-65
pubmed: 20202938
Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):133-44
pubmed: 20124693
Biol Chem. 2017 Aug 28;398(9):975-994
pubmed: 28253193
Nat Struct Biol. 1996 Aug;3(8):671-5
pubmed: 8756323
J Biol Chem. 2004 Mar 19;279(12):11146-55
pubmed: 14709555
J Mol Biol. 2007 Sep 21;372(3):774-97
pubmed: 17681537
J Invest Dermatol. 2007 May;127(5):1115-25
pubmed: 17195012
Methods Enzymol. 2003;374:461-91
pubmed: 14696385
Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501
pubmed: 20383002
FEBS J. 2010 Apr;277(7):1726-37
pubmed: 20175878
J Mol Biol. 1993 Feb 20;229(4):945-68
pubmed: 8445658
Nucleic Acids Res. 2015 Jul 1;43(W1):W389-94
pubmed: 25883141
J Biol Chem. 1989 Aug 25;264(24):14121-8
pubmed: 2760061
Biol Chem. 2003 May;384(5):825-31
pubmed: 12817480
J Synchrotron Radiat. 2012 May;19(Pt 3):455-61
pubmed: 22514185
Acta Crystallogr D Biol Crystallogr. 2012 Apr;68(Pt 4):352-67
pubmed: 22505256
Acta Crystallogr D Biol Crystallogr. 2012 Apr;68(Pt 4):368-80
pubmed: 22505257
J Cell Biol. 2012 Apr 2;197(1):37-44
pubmed: 22472438
EMBO J. 1988 Aug;7(8):2593-9
pubmed: 3191914
Nature. 1992 Jul 9;358(6382):164-7
pubmed: 1319561
Biochem Mol Biol Int. 1996 Aug;39(5):1023-8
pubmed: 8866020
Hum Reprod. 2016 Mar;31(3):630-7
pubmed: 26759143
BMC Bioinformatics. 2004 Jun 04;5:69
pubmed: 15180909
J Biol Chem. 2010 Apr 30;285(18):13951-7
pubmed: 20202937
Arch Biochem Biophys. 1974 Sep;164(1):326-31
pubmed: 4139931
Sci Rep. 2019 Jan 24;9(1):546
pubmed: 30679641
Genome Inform Ser Workshop Genome Inform. 2000;11:161-71
pubmed: 11700597
Proc Natl Acad Sci U S A. 2005 Mar 15;102(11):3978-83
pubmed: 15738388
J Synchrotron Radiat. 2014 Jul;21(Pt 4):679-89
pubmed: 24971961
J Biol Chem. 1993 Aug 25;268(24):17750-3
pubmed: 7688730
Biol Chem. 2014 Oct;395(10):1195-9
pubmed: 25205729
J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674
pubmed: 19461840
Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):331-7
pubmed: 21460451
Mol Hum Reprod. 2017 Sep 1;23(9):607-616
pubmed: 28911209
Nat Protoc. 2012 Jul 19;7(8):1511-22
pubmed: 22814390
Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13419-24
pubmed: 12370423
EMBO J. 1990 Jun;9(6):1939-47
pubmed: 2347312
Biochem J. 1986 Mar 1;234(2):429-34
pubmed: 3521586
Biochem Biophys Res Commun. 1967 Apr 20;27(2):157-62
pubmed: 6035483
Biol Chem. 2012 Oct;393(10):1027-41
pubmed: 23092796
Nucleic Acids Res. 2004 Mar 19;32(5):1792-7
pubmed: 15034147
Mol Biol Evol. 2010 Feb;27(2):221-4
pubmed: 19854763
Mol Hum Reprod. 2017 Jan;23(1):34-44
pubmed: 27733488
Biochemistry. 2010 Oct 5;49(39):8599-607
pubmed: 20806899

Auteurs

Anna Cuppari (A)

Proteolysis Laboratory, Department of Structural Biology, Molecular Biology Institute of Barcelona, CSIC, Barcelona Science Park, Helix Building, c/o Baldiri Reixac 15-21, E-08028 Barcelona, Catalonia, Spain.

Hagen Körschgen (H)

Institute of Molecular Physiology, Cell and Matrix Biology, Johannes Gutenberg-University Mainz, Johann-Joachim-Becher-Weg 7, D-55128 Mainz, Germany.

Dirk Fahrenkamp (D)

Department of Biosciences and Nutrition and Center for Innovative Medicine, Karolinska Institutet, Blickagången 16, SE-141 83 Huddinge, Sweden.

Carlo Schmitz (C)

Biointerface Laboratory, Helmholtz Institute for Biomedical Engineering, RWTH Aachen University Medical Faculty, Pauwelsstrasse 30, D-52074 Aachen, Germany.

Tibisay Guevara (T)

Proteolysis Laboratory, Department of Structural Biology, Molecular Biology Institute of Barcelona, CSIC, Barcelona Science Park, Helix Building, c/o Baldiri Reixac 15-21, E-08028 Barcelona, Catalonia, Spain.

Konstantin Karmilin (K)

Institute of Molecular Physiology, Cell and Matrix Biology, Johannes Gutenberg-University Mainz, Johann-Joachim-Becher-Weg 7, D-55128 Mainz, Germany.

Michael Kuske (M)

Institute of Molecular Physiology, Cell and Matrix Biology, Johannes Gutenberg-University Mainz, Johann-Joachim-Becher-Weg 7, D-55128 Mainz, Germany.

Mario Olf (M)

Institute of Molecular Physiology, Cell and Matrix Biology, Johannes Gutenberg-University Mainz, Johann-Joachim-Becher-Weg 7, D-55128 Mainz, Germany.

Eileen Dietzel (E)

Department of Biosciences and Nutrition and Center for Innovative Medicine, Karolinska Institutet, Blickagången 16, SE-141 83 Huddinge, Sweden.

Irene Yiallouros (I)

Institute of Molecular Physiology, Cell and Matrix Biology, Johannes Gutenberg-University Mainz, Johann-Joachim-Becher-Weg 7, D-55128 Mainz, Germany.

Daniele de Sanctis (D)

ESRF - The European Synchrotron, 71 Rue Jules Horowitz, F-38000 Grenoble, France.

Theodoros Goulas (T)

Proteolysis Laboratory, Department of Structural Biology, Molecular Biology Institute of Barcelona, CSIC, Barcelona Science Park, Helix Building, c/o Baldiri Reixac 15-21, E-08028 Barcelona, Catalonia, Spain.

Ralf Weiskirchen (R)

Institute of Molecular Pathobiochemistry, Experimental Gene Therapy and Clinical Chemistry, RWTH Aachen University Hospital, Pauwelsstrasse 30, D-52074 Aachen, Germany.

Willi Jahnen-Dechent (W)

Biointerface Laboratory, Helmholtz Institute for Biomedical Engineering, RWTH Aachen University Medical Faculty, Pauwelsstrasse 30, D-52074 Aachen, Germany.

Julia Floehr (J)

Biointerface Laboratory, Helmholtz Institute for Biomedical Engineering, RWTH Aachen University Medical Faculty, Pauwelsstrasse 30, D-52074 Aachen, Germany.

Walter Stoecker (W)

Institute of Molecular Physiology, Cell and Matrix Biology, Johannes Gutenberg-University Mainz, Johann-Joachim-Becher-Weg 7, D-55128 Mainz, Germany.

Luca Jovine (L)

Department of Biosciences and Nutrition and Center for Innovative Medicine, Karolinska Institutet, Blickagången 16, SE-141 83 Huddinge, Sweden.

F Xavier Gomis-Rüth (FX)

Proteolysis Laboratory, Department of Structural Biology, Molecular Biology Institute of Barcelona, CSIC, Barcelona Science Park, Helix Building, c/o Baldiri Reixac 15-21, E-08028 Barcelona, Catalonia, Spain.

Classifications MeSH