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1eqk

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(New page: 200px<br /><applet load="1eqk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eqk" /> '''SOLUTION STRUCTURE OF ORYZACYSTATIN-I, A CYS...)
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'''SOLUTION STRUCTURE OF ORYZACYSTATIN-I, A CYSTEINE PROTEINASE INHIBITOR OF THE RICE, ORYZA SATIVA L. JAPONICA'''<br />
'''SOLUTION STRUCTURE OF ORYZACYSTATIN-I, A CYSTEINE PROTEINASE INHIBITOR OF THE RICE, ORYZA SATIVA L. JAPONICA'''<br />
==Overview==
==Overview==
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The three-dimensional structure of oryzacystatin-I, a cysteine proteinase, inhibitor of the rice, Oryza sativa L. japonica, has been determined in, solution at pH 6.8 and 25 degrees C by (1)H and (15)N NMR spectroscopy., The main body (Glu13-Asp97) of oryzacystatin-I is well-defined and, consists of an alpha-helix and a five-stranded antiparallel beta-sheet, while the N- and C-terminal regions (Ser2-Val12 and Ala98-Ala102) are less, defined. The helix-sheet architechture of oryzacystatin-I is stabilized by, a hydrophobic cluster formed between the alpha-helix and the beta-sheet, and is considerably similar to that of monellin, a sweet-tasting protein, from an African berry, as well as those of the animal cystatins studied, e.g., chicken egg white cystatin and human stefins A and B (also referred, to as human cystatins A and B). Detailed structural comparison indicates, that oryzacystatin-I is more similar to chicken cystatin, which belongs to, the type-2 animal cystatins, than to human stefins A and B, which belong, to the type-1 animal cystatins, despite different loop length.
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The three-dimensional structure of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica, has been determined in solution at pH 6.8 and 25 degrees C by (1)H and (15)N NMR spectroscopy. The main body (Glu13-Asp97) of oryzacystatin-I is well-defined and consists of an alpha-helix and a five-stranded antiparallel beta-sheet, while the N- and C-terminal regions (Ser2-Val12 and Ala98-Ala102) are less defined. The helix-sheet architechture of oryzacystatin-I is stabilized by a hydrophobic cluster formed between the alpha-helix and the beta-sheet and is considerably similar to that of monellin, a sweet-tasting protein from an African berry, as well as those of the animal cystatins studied, e.g., chicken egg white cystatin and human stefins A and B (also referred to as human cystatins A and B). Detailed structural comparison indicates that oryzacystatin-I is more similar to chicken cystatin, which belongs to the type-2 animal cystatins, than to human stefins A and B, which belong to the type-1 animal cystatins, despite different loop length.
==About this Structure==
==About this Structure==
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1EQK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryza_sativa_japonica_group Oryza sativa japonica group]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EQK OCA].
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1EQK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryza_sativa_japonica_group Oryza sativa japonica group]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQK OCA].
==Reference==
==Reference==
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[[Category: phytocystatin family]]
[[Category: phytocystatin family]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:13:55 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:33 2008''

Revision as of 10:30, 21 February 2008


1eqk

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SOLUTION STRUCTURE OF ORYZACYSTATIN-I, A CYSTEINE PROTEINASE INHIBITOR OF THE RICE, ORYZA SATIVA L. JAPONICA

Overview

The three-dimensional structure of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica, has been determined in solution at pH 6.8 and 25 degrees C by (1)H and (15)N NMR spectroscopy. The main body (Glu13-Asp97) of oryzacystatin-I is well-defined and consists of an alpha-helix and a five-stranded antiparallel beta-sheet, while the N- and C-terminal regions (Ser2-Val12 and Ala98-Ala102) are less defined. The helix-sheet architechture of oryzacystatin-I is stabilized by a hydrophobic cluster formed between the alpha-helix and the beta-sheet and is considerably similar to that of monellin, a sweet-tasting protein from an African berry, as well as those of the animal cystatins studied, e.g., chicken egg white cystatin and human stefins A and B (also referred to as human cystatins A and B). Detailed structural comparison indicates that oryzacystatin-I is more similar to chicken cystatin, which belongs to the type-2 animal cystatins, than to human stefins A and B, which belong to the type-1 animal cystatins, despite different loop length.

About this Structure

1EQK is a Single protein structure of sequence from Oryza sativa japonica group. Full crystallographic information is available from OCA.

Reference

Three-dimensional solution structure of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica., Nagata K, Kudo N, Abe K, Arai S, Tanokura M, Biochemistry. 2000 Dec 5;39(48):14753-60. PMID:11101290

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