1c2a: Difference between revisions
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'''CRYSTAL STRUCTURE OF BARLEY BBI''' | {{Structure | ||
|PDB= 1c2a |SIZE=350|CAPTION= <scene name='initialview01'>1c2a</scene>, resolution 1.9Å | |||
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|LIGAND= | |||
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'''CRYSTAL STRUCTURE OF BARLEY BBI''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1C2A is a [ | 1C2A is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C2A OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of a 16 kDa double-headed Bowman-Birk trypsin inhibitor from barley seeds at 1.9 A resolution., Song HK, Kim YS, Yang JK, Moon J, Lee JY, Suh SW, J Mol Biol. 1999 Nov 12;293(5):1133-44. PMID:[http:// | Crystal structure of a 16 kDa double-headed Bowman-Birk trypsin inhibitor from barley seeds at 1.9 A resolution., Song HK, Kim YS, Yang JK, Moon J, Lee JY, Suh SW, J Mol Biol. 1999 Nov 12;293(5):1133-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10547291 10547291] | ||
[[Category: Hordeum vulgare]] | [[Category: Hordeum vulgare]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: all-beta structure]] | [[Category: all-beta structure]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:18:53 2008'' | ||
Revision as of 11:18, 20 March 2008
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CRYSTAL STRUCTURE OF BARLEY BBI
OverviewOverview
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.
About this StructureAbout this Structure
1C2A is a Single protein structure of sequence from Hordeum vulgare. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a 16 kDa double-headed Bowman-Birk trypsin inhibitor from barley seeds at 1.9 A resolution., Song HK, Kim YS, Yang JK, Moon J, Lee JY, Suh SW, J Mol Biol. 1999 Nov 12;293(5):1133-44. PMID:10547291
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