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| - | [[Image:1o0e.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1o0e| PDB=1o0e | SCENE= }} | | {{STRUCTURE_1o0e| PDB=1o0e | SCENE= }} |
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| - | '''1.9 Angstrom Crystal Structure of a plant cysteine protease Ervatamin C'''
| + | ===1.9 Angstrom Crystal Structure of a plant cysteine protease Ervatamin C=== |
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| - | ==Overview==
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| - | Ervatamin C is an unusually stable cysteine protease from the medicinal plant Ervatamia coronaria belonging to the papain family. Though it cleaves denatured natural proteins with high specific activity, its activity toward some small synthetic substrates is found to be insignificant. The three-dimensional structure and amino acid sequence of the protein have been determined from X-ray diffraction data at 1.9 A (R = 17.7% and R(free) = 19.0%). The overall structure of ervatamin C is similar to those of other homologous cysteine proteases of the family, folding into two distinct left and right domains separated by an active site cleft. However, substitution of a few amino acid residues, which are conserved in the other members of the family, has been observed in both the domains and also at the region of the interdomain cleft. Consequently, the number of intra- and interdomain hydrogen-bonding interactions is enhanced in the structure of ervatamin C. Moreover, a unique disulfide bond has been identified in the right domain of the structure, in addition to the three conserved disulfide bridges present in the papain family. All these factors contribute to an increase in the stability of ervatamin C. In this enzyme, the nature of the S2 subsite, which is the primary determinant of specificity of these proteases, is similar to that of papain, but at the S3 subsite, Ala67 replaces an aromatic residue, and has the effect of eliminating sufficient hydrophobic interactions required for S3-P3 stabilization. This provides the possible explanation for the lower activity of ervatamin C toward the small substrate/inhibitor. This substitution, however, does not affect the binding of denatured natural protein substrates to the enzyme significantly, as there exist a number of additional interactions at the enzyme-substrate interface outside the active site cleft.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_14769029}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 14769029 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_14769029}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Stable at ph 2-12]] | | [[Category: Stable at ph 2-12]] |
| | [[Category: Two domain]] | | [[Category: Two domain]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:12:29 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:58:39 2008'' |
Revision as of 04:58, 29 July 2008
Template:STRUCTURE 1o0e
1.9 Angstrom Crystal Structure of a plant cysteine protease Ervatamin C
Template:ABSTRACT PUBMED 14769029
About this Structure
1O0E is a Single protein structure of sequence from Tabernaemontana divaricata. Full crystallographic information is available from OCA.
Reference
Structural basis of the unusual stability and substrate specificity of ervatamin C, a plant cysteine protease from Ervatamia coronaria., Thakurta PG, Biswas S, Chakrabarti C, Sundd M, Jagannadham MV, Dattagupta JK, Biochemistry. 2004 Feb 17;43(6):1532-40. PMID:14769029
Page seeded by OCA on Tue Jul 29 07:58:39 2008
