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1pbi
From Proteopedia
(New page: 200px<br /><applet load="1pbi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pbi, resolution 2.70Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1pbi.jpg|left|200px]]<br /><applet load="1pbi" size=" | + | [[Image:1pbi.jpg|left|200px]]<br /><applet load="1pbi" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pbi, resolution 2.70Å" /> | caption="1pbi, resolution 2.70Å" /> | ||
'''CRYSTAL STRUCTURE OF A BOWMAN-BIRK INHIBITOR FROM PEA SEEDS'''<br /> | '''CRYSTAL STRUCTURE OF A BOWMAN-BIRK INHIBITOR FROM PEA SEEDS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The trypsin/chymotrypsin inhibitors from winter pea seeds (PsTI) are | + | The trypsin/chymotrypsin inhibitors from winter pea seeds (PsTI) are members of the Bowman-Birk protease inhibitor (BBPI) family. The crystal structure of the isoform PsTI-IVb was determined by molecular replacement at 2.7 A resolution using the X-ray co-ordinates of the soybean inhibitor as a search model. The inhibitor crystallized with a nearly perfect 2-fold symmetric dimer in the asymmetric unit. Although the overall structure is very similar to that seen in other BBPIs, there are notable new structural features. Unlike the previously reported X-ray structures of BBPIs, the structure of PsTI-IVb includes the C-terminal segment of the molecule. The C-terminal tail of each subunit is partly beta-stranded and interacts with the 2-fold symmetry-related subunit, forming a beta-sheet with strands A and B of this subunit. The dimer is mainly stabilized by a large internal hydrogen-bonded network surrounded by two hydrophobic links. Fluorescence anisotropy decay measurements show that residues Tyr59 and Tyr43 are mobile in the picosecond time scale with a large amplitude. The fluorescence study and a molecular model of the simultaneous binding of PsTI-IVb to porcine trypsin and bovine chymotrypsin are compatible only with a monomeric state of the functional molecule in solution. |
==About this Structure== | ==About this Structure== | ||
| - | 1PBI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http:// | + | 1PBI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PBI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Brunie, S.]] | [[Category: Brunie, S.]] | ||
| - | [[Category: Sierra, I | + | [[Category: Sierra, I Li De La.]] |
[[Category: bowman-birk inhibitor]] | [[Category: bowman-birk inhibitor]] | ||
[[Category: chymotrypsin inhibitor]] | [[Category: chymotrypsin inhibitor]] | ||
[[Category: trypsin inhibitor]] | [[Category: trypsin inhibitor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:14 2008'' |
Revision as of 12:27, 21 February 2008
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CRYSTAL STRUCTURE OF A BOWMAN-BIRK INHIBITOR FROM PEA SEEDS
Overview
The trypsin/chymotrypsin inhibitors from winter pea seeds (PsTI) are members of the Bowman-Birk protease inhibitor (BBPI) family. The crystal structure of the isoform PsTI-IVb was determined by molecular replacement at 2.7 A resolution using the X-ray co-ordinates of the soybean inhibitor as a search model. The inhibitor crystallized with a nearly perfect 2-fold symmetric dimer in the asymmetric unit. Although the overall structure is very similar to that seen in other BBPIs, there are notable new structural features. Unlike the previously reported X-ray structures of BBPIs, the structure of PsTI-IVb includes the C-terminal segment of the molecule. The C-terminal tail of each subunit is partly beta-stranded and interacts with the 2-fold symmetry-related subunit, forming a beta-sheet with strands A and B of this subunit. The dimer is mainly stabilized by a large internal hydrogen-bonded network surrounded by two hydrophobic links. Fluorescence anisotropy decay measurements show that residues Tyr59 and Tyr43 are mobile in the picosecond time scale with a large amplitude. The fluorescence study and a molecular model of the simultaneous binding of PsTI-IVb to porcine trypsin and bovine chymotrypsin are compatible only with a monomeric state of the functional molecule in solution.
About this Structure
1PBI is a Single protein structure of sequence from Pisum sativum. Full crystallographic information is available from OCA.
Reference
Dimeric crystal structure of a Bowman-Birk protease inhibitor from pea seeds., Li de la Sierra I, Quillien L, Flecker P, Gueguen J, Brunie S, J Mol Biol. 1999 Jan 22;285(3):1195-207. PMID:9887273
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