Structure of a post-translationally processed heterodimeric double-headed Kunitz-type serineprotease inhibitor from potato

E.M. Meulenbroek, E.A.J. Thomassen, L.A.M. Pouvreau, J.P. Abrahams, H. Gruppen, N.S. Pannu

Research output: Contribution to journalArticleAcademicpeer-review

13 Citations (Scopus)

Abstract

Potato serine protease inhibitor (PSPI) constitutes about 22% of the total amount of proteins in potato tubers (cv. Elkana), making it the most abundant protease inhibitor in the plant. PSPI is a heterodimeric double-headed Kunitz-type serine protease inhibitor that can tightly and simultaneously bind two serine proteases by mimicking the substrate of the enzyme with its reactive-site loops. Here, the crystal structure of PSPI is reported, representing the first heterodimeric doubleheaded Kunitz-type serine protease inhibitor structure to be determined. PSPI has a-trefoil fold and, based on the structure, two reactive-site loops bearing residues Phe75 and Lys95 were identified.
LanguageEnglish
Pages794-799
JournalActa Crystallographica Section D-Biological Crystallography
Volume68
Issue number7
DOIs
Publication statusPublished - 2012

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Serine Proteinase Inhibitors
Solanum tuberosum
Catalytic Domain
Serine Proteases
Protease Inhibitors
Enzymes
Proteins

Keywords

  • macromolecular crystallography
  • chymotrypsin inhibitor
  • molecular-replacement
  • proteinase-inhibitors
  • crystal-structure
  • reactive-site
  • cv elkana
  • refinement
  • seeds

Cite this

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title = "Structure of a post-translationally processed heterodimeric double-headed Kunitz-type serineprotease inhibitor from potato",
abstract = "Potato serine protease inhibitor (PSPI) constitutes about 22{\%} of the total amount of proteins in potato tubers (cv. Elkana), making it the most abundant protease inhibitor in the plant. PSPI is a heterodimeric double-headed Kunitz-type serine protease inhibitor that can tightly and simultaneously bind two serine proteases by mimicking the substrate of the enzyme with its reactive-site loops. Here, the crystal structure of PSPI is reported, representing the first heterodimeric doubleheaded Kunitz-type serine protease inhibitor structure to be determined. PSPI has a-trefoil fold and, based on the structure, two reactive-site loops bearing residues Phe75 and Lys95 were identified.",
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pages = "794--799",
journal = "Acta Crystallographica Section D-Biological Crystallography",
issn = "0907-4449",
publisher = "International Union of Crystallography",
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Structure of a post-translationally processed heterodimeric double-headed Kunitz-type serineprotease inhibitor from potato. / Meulenbroek, E.M.; Thomassen, E.A.J.; Pouvreau, L.A.M.; Abrahams, J.P.; Gruppen, H.; Pannu, N.S.

In: Acta Crystallographica Section D-Biological Crystallography, Vol. 68, No. 7, 2012, p. 794-799.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Structure of a post-translationally processed heterodimeric double-headed Kunitz-type serineprotease inhibitor from potato

AU - Meulenbroek, E.M.

AU - Thomassen, E.A.J.

AU - Pouvreau, L.A.M.

AU - Abrahams, J.P.

AU - Gruppen, H.

AU - Pannu, N.S.

PY - 2012

Y1 - 2012

N2 - Potato serine protease inhibitor (PSPI) constitutes about 22% of the total amount of proteins in potato tubers (cv. Elkana), making it the most abundant protease inhibitor in the plant. PSPI is a heterodimeric double-headed Kunitz-type serine protease inhibitor that can tightly and simultaneously bind two serine proteases by mimicking the substrate of the enzyme with its reactive-site loops. Here, the crystal structure of PSPI is reported, representing the first heterodimeric doubleheaded Kunitz-type serine protease inhibitor structure to be determined. PSPI has a-trefoil fold and, based on the structure, two reactive-site loops bearing residues Phe75 and Lys95 were identified.

AB - Potato serine protease inhibitor (PSPI) constitutes about 22% of the total amount of proteins in potato tubers (cv. Elkana), making it the most abundant protease inhibitor in the plant. PSPI is a heterodimeric double-headed Kunitz-type serine protease inhibitor that can tightly and simultaneously bind two serine proteases by mimicking the substrate of the enzyme with its reactive-site loops. Here, the crystal structure of PSPI is reported, representing the first heterodimeric doubleheaded Kunitz-type serine protease inhibitor structure to be determined. PSPI has a-trefoil fold and, based on the structure, two reactive-site loops bearing residues Phe75 and Lys95 were identified.

KW - macromolecular crystallography

KW - chymotrypsin inhibitor

KW - molecular-replacement

KW - proteinase-inhibitors

KW - crystal-structure

KW - reactive-site

KW - cv elkana

KW - refinement

KW - seeds

U2 - 10.1107/S090744491201222X

DO - 10.1107/S090744491201222X

M3 - Article

VL - 68

SP - 794

EP - 799

JO - Acta Crystallographica Section D-Biological Crystallography

T2 - Acta Crystallographica Section D-Biological Crystallography

JF - Acta Crystallographica Section D-Biological Crystallography

SN - 0907-4449

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