2ab9

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(New page: 200px<br /><applet load="2ab9" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ab9" /> '''Discovery, structural determination and proc...)
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[[Image:2ab9.gif|left|200px]]<br /><applet load="2ab9" size="350" color="white" frame="true" align="right" spinBox="true"
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'''Discovery, structural determination and processing of the precursor protein that produces the cyclic trypsin inhibitor SFTI-1'''<br />
'''Discovery, structural determination and processing of the precursor protein that produces the cyclic trypsin inhibitor SFTI-1'''<br />
==Overview==
==Overview==
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Backbone-cyclized proteins are becoming increasingly well known, although, the mechanism by which they are processed from linear precursors is poorly, understood. In this report the sequence and structure of the linear, precursor of a cyclic trypsin inhibitor, sunflower trypsin inhibitor 1, (SFTI-1) from sunflower seeds, is described. The structure indicates that, the major elements of the reactive site loop of SFTI-1 are present before, processing. This may have importance for a protease-mediated cyclizing, reaction as the rigidity of SFTI-1 may drive the equilibrium of the, reaction catalyzed by proteolytic enzymes toward the formation of a, peptide bond rather than the normal cleavage reaction. The occurrence of, residues in the SFTI-1 precursor susceptible to cleavage by asparaginyl, proteases strengthens theories that involve this enzyme in the processing, of SFTI-1 and further implicates it in the processing of another family of, plant cyclic proteins, the cyclotides. The precursor reported here also, indicates that despite strong active site sequence homology, SFTI-1 has no, other similarities with the Bowman-Birk trypsin inhibitors, presenting, interesting evolutionary questions.
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Backbone-cyclized proteins are becoming increasingly well known, although the mechanism by which they are processed from linear precursors is poorly understood. In this report the sequence and structure of the linear precursor of a cyclic trypsin inhibitor, sunflower trypsin inhibitor 1 (SFTI-1) from sunflower seeds, is described. The structure indicates that the major elements of the reactive site loop of SFTI-1 are present before processing. This may have importance for a protease-mediated cyclizing reaction as the rigidity of SFTI-1 may drive the equilibrium of the reaction catalyzed by proteolytic enzymes toward the formation of a peptide bond rather than the normal cleavage reaction. The occurrence of residues in the SFTI-1 precursor susceptible to cleavage by asparaginyl proteases strengthens theories that involve this enzyme in the processing of SFTI-1 and further implicates it in the processing of another family of plant cyclic proteins, the cyclotides. The precursor reported here also indicates that despite strong active site sequence homology, SFTI-1 has no other similarities with the Bowman-Birk trypsin inhibitors, presenting interesting evolutionary questions.
==About this Structure==
==About this Structure==
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2AB9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helianthus_annuus Helianthus annuus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AB9 OCA].
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2AB9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helianthus_annuus Helianthus annuus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AB9 OCA].
==Reference==
==Reference==
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[[Category: Helianthus annuus]]
[[Category: Helianthus annuus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Craik, D.J.]]
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[[Category: Craik, D J.]]
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[[Category: Foley, F.M.]]
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[[Category: Foley, F M.]]
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[[Category: Mulvenna, J.P.]]
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[[Category: Mulvenna, J P.]]
[[Category: beta-sheet]]
[[Category: beta-sheet]]
[[Category: protein]]
[[Category: protein]]
[[Category: random coil]]
[[Category: random coil]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:02:03 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:25:44 2008''

Revision as of 14:25, 21 February 2008


2ab9

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Discovery, structural determination and processing of the precursor protein that produces the cyclic trypsin inhibitor SFTI-1

Overview

Backbone-cyclized proteins are becoming increasingly well known, although the mechanism by which they are processed from linear precursors is poorly understood. In this report the sequence and structure of the linear precursor of a cyclic trypsin inhibitor, sunflower trypsin inhibitor 1 (SFTI-1) from sunflower seeds, is described. The structure indicates that the major elements of the reactive site loop of SFTI-1 are present before processing. This may have importance for a protease-mediated cyclizing reaction as the rigidity of SFTI-1 may drive the equilibrium of the reaction catalyzed by proteolytic enzymes toward the formation of a peptide bond rather than the normal cleavage reaction. The occurrence of residues in the SFTI-1 precursor susceptible to cleavage by asparaginyl proteases strengthens theories that involve this enzyme in the processing of SFTI-1 and further implicates it in the processing of another family of plant cyclic proteins, the cyclotides. The precursor reported here also indicates that despite strong active site sequence homology, SFTI-1 has no other similarities with the Bowman-Birk trypsin inhibitors, presenting interesting evolutionary questions.

About this Structure

2AB9 is a Single protein structure of sequence from Helianthus annuus. Full crystallographic information is available from OCA.

Reference

Discovery, structural determination, and putative processing of the precursor protein that produces the cyclic trypsin inhibitor sunflower trypsin inhibitor 1., Mulvenna JP, Foley FM, Craik DJ, J Biol Chem. 2005 Sep 16;280(37):32245-53. Epub 2005 Jul 21. PMID:16036912

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