1C2A

CRYSTAL STRUCTURE OF BARLEY BBI

Summary for 1C2A

• Entry DOI: 10.2210/pdb1c2a/pdb
• Related: 1PI2
• Descriptor: BOWMAN-BIRK TRYPSIN INHIBITOR (2 entities in total)
• Functional Keywords: all-beta structure, hydrolase inhibitor
• Biological source: Hordeum vulgare
• Total number of polymer chains: 1
• Total formula weight: 13420.77

Authors

Song, H.K.,Kim, Y.S.,Yang, J.K.,Moon, J.,Lee, J.Y.,Suh, S.W. (deposition date: 1999-07-23, release date: 1999-12-29, Last modification date: 2024-10-30)

Primary citation

Song, H.K.,Kim, Y.S.,Yang, J.K.,Moon, J.,Lee, J.Y.,Suh, S.W.
Crystal structure of a 16 kDa double-headed Bowman-Birk trypsin inhibitor from barley seeds at 1.9 A resolution.
J.Mol.Biol., 293:1133-1144, 1999

PubMed 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 A 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 beta-strands and the loops connecting these beta-strands but it lacks alpha-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 A 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.

PubMed: 10547291
DOI: 10.1006/jmbi.1999.3239

Experimental method

X-RAY DIFFRACTION (1.9 Å)