Crystal structure of a 16 kDa double-headed Bowman-Birk trypsin inhibitor from barley seeds at 1.9 Å resolution

Hyun Kyu Song, Young Sil Kim, Jin Kuk Yang, Jinho Moon, Jae Young Lee, Se Won Suh

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

The Bowman-Birk trypsin inhibitor from barley seeds (BBBI) consists of 125 amino acid residues with two inhibitory loops. Its crystal structure in the free state has been determined by the multiwavelength anomalous diffraction (MAD) method and has been refined to a crystallographic R-value of 19.1% for 8.0-1.9 Å data. This is the first report on the structure of a 16 kDa double-headed Bowman-Birk inhibitor (BBI) from monocotyledonous plants and provides the highest resolution picture of a BBI to date. The BBBI structure consists of 11 β-strands and the loops connecting these β-strands but it lacks α-helices. BBBI folds into two compact domains of similar tertiary structure. Each domain shares the same overall fold with 8 kDa dicotyledonous BBIs. The five disulfide bridges in each domain are a subset of the seven disulfide bridges in 8 kDa dicotyledonous BBIs. Two buried water molecules form hydrogen bonds to backbone atoms in the core of each domain. One interesting feature of this two-domain inhibitor structure is that the two P1 residues (Arg17 and Arg76) are approximately 40 Å apart, allowing the two reactive-site loops to bind to and to inhibit two trypsin molecules simultaneously and independently. The conformations of the reactive-site loops of BBBI are highly similar to those of other substrate-like inhibitors. This structure provides the framework for modeling of the 1:2 complex between BBBI and trypsin.

Original languageEnglish
Pages (from-to)1133-1144
Number of pages12
JournalJournal of Molecular Biology
Volume293
Issue number5
DOIs
Publication statusPublished - 1999 Nov 12
Externally publishedYes

Fingerprint

Trypsin Inhibitors
Hordeum
Disulfides
Trypsin
Catalytic Domain
Seeds
Hydrogen
Amino Acids
Water

Keywords

  • Bowman-Birk trypsin inhibitor
  • Double-headed inhibitor
  • Gene duplication
  • Monocotyledonous plant
  • Reactive-site loop

ASJC Scopus subject areas

  • Virology

Cite this

Crystal structure of a 16 kDa double-headed Bowman-Birk trypsin inhibitor from barley seeds at 1.9 Å resolution. / Song, Hyun Kyu; Kim, Young Sil; Yang, Jin Kuk; Moon, Jinho; Lee, Jae Young; Suh, Se Won.

In: Journal of Molecular Biology, Vol. 293, No. 5, 12.11.1999, p. 1133-1144.

Research output: Contribution to journalArticle

Song, Hyun Kyu ; Kim, Young Sil ; Yang, Jin Kuk ; Moon, Jinho ; Lee, Jae Young ; Suh, Se Won. / Crystal structure of a 16 kDa double-headed Bowman-Birk trypsin inhibitor from barley seeds at 1.9 Å resolution. In: Journal of Molecular Biology. 1999 ; Vol. 293, No. 5. pp. 1133-1144.
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abstract = "The Bowman-Birk trypsin inhibitor from barley seeds (BBBI) consists of 125 amino acid residues with two inhibitory loops. Its crystal structure in the free state has been determined by the multiwavelength anomalous diffraction (MAD) method and has been refined to a crystallographic R-value of 19.1{\%} for 8.0-1.9 {\AA} data. This is the first report on the structure of a 16 kDa double-headed Bowman-Birk inhibitor (BBI) from monocotyledonous plants and provides the highest resolution picture of a BBI to date. The BBBI structure consists of 11 β-strands and the loops connecting these β-strands but it lacks α-helices. BBBI folds into two compact domains of similar tertiary structure. Each domain shares the same overall fold with 8 kDa dicotyledonous BBIs. The five disulfide bridges in each domain are a subset of the seven disulfide bridges in 8 kDa dicotyledonous BBIs. Two buried water molecules form hydrogen bonds to backbone atoms in the core of each domain. One interesting feature of this two-domain inhibitor structure is that the two P1 residues (Arg17 and Arg76) are approximately 40 {\AA} apart, allowing the two reactive-site loops to bind to and to inhibit two trypsin molecules simultaneously and independently. The conformations of the reactive-site loops of BBBI are highly similar to those of other substrate-like inhibitors. This structure provides the framework for modeling of the 1:2 complex between BBBI and trypsin.",
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AB - The Bowman-Birk trypsin inhibitor from barley seeds (BBBI) consists of 125 amino acid residues with two inhibitory loops. Its crystal structure in the free state has been determined by the multiwavelength anomalous diffraction (MAD) method and has been refined to a crystallographic R-value of 19.1% for 8.0-1.9 Å data. This is the first report on the structure of a 16 kDa double-headed Bowman-Birk inhibitor (BBI) from monocotyledonous plants and provides the highest resolution picture of a BBI to date. The BBBI structure consists of 11 β-strands and the loops connecting these β-strands but it lacks α-helices. BBBI folds into two compact domains of similar tertiary structure. Each domain shares the same overall fold with 8 kDa dicotyledonous BBIs. The five disulfide bridges in each domain are a subset of the seven disulfide bridges in 8 kDa dicotyledonous BBIs. Two buried water molecules form hydrogen bonds to backbone atoms in the core of each domain. One interesting feature of this two-domain inhibitor structure is that the two P1 residues (Arg17 and Arg76) are approximately 40 Å apart, allowing the two reactive-site loops to bind to and to inhibit two trypsin molecules simultaneously and independently. The conformations of the reactive-site loops of BBBI are highly similar to those of other substrate-like inhibitors. This structure provides the framework for modeling of the 1:2 complex between BBBI and trypsin.

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