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| - | [[Image:1c2a.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1c2a| PDB=1c2a | SCENE= }} | | {{STRUCTURE_1c2a| PDB=1c2a | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF BARLEY BBI'''
| + | ===CRYSTAL STRUCTURE OF BARLEY BBI=== |
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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_10547291}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10547291 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10547291}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Yang, J K.]] | | [[Category: Yang, J K.]] |
| | [[Category: All-beta structure]] | | [[Category: All-beta structure]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:14:52 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:06:54 2008'' |
Revision as of 17:06, 30 June 2008
Template:STRUCTURE 1c2a
CRYSTAL STRUCTURE OF BARLEY BBI
Template:ABSTRACT PUBMED 10547291
About this Structure
1C2A is a Single protein structure of sequence from Hordeum vulgare. Full crystallographic information is available from OCA.
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:10547291
Page seeded by OCA on Mon Jun 30 20:06:54 2008
