1qdm
From Proteopedia
(New page: 200px<br /><applet load="1qdm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qdm, resolution 2.3Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1qdm.gif|left|200px]]<br /><applet load="1qdm" size=" | + | [[Image:1qdm.gif|left|200px]]<br /><applet load="1qdm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qdm, resolution 2.3Å" /> | caption="1qdm, resolution 2.3Å" /> | ||
'''CRYSTAL STRUCTURE OF PROPHYTEPSIN, A ZYMOGEN OF A BARLEY VACUOLAR ASPARTIC PROTEINASE.'''<br /> | '''CRYSTAL STRUCTURE OF PROPHYTEPSIN, A ZYMOGEN OF A BARLEY VACUOLAR ASPARTIC PROTEINASE.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We determined at 2.3 A resolution the crystal structure of prophytepsin, a | + | We determined at 2.3 A resolution the crystal structure of prophytepsin, a zymogen of a barley vacuolar aspartic proteinase. In addition to the classical pepsin-like bilobal main body of phytepsin, we also traced most of the propeptide, as well as an independent plant-specific domain, never before described in structural terms. The structure revealed that, in addition to the propeptide, 13 N-terminal residues of the mature phytepsin are essential for inactivation of the enzyme. Comparison of the plant-specific domain with NK-lysin indicates that these two saposin-like structures are closely related, suggesting that all saposins and saposin-like domains share a common topology. Structural analysis of prophytepsin led to the identification of a putative membrane receptor-binding site involved in Golgi-mediated transport to vacuoles. |
==About this Structure== | ==About this Structure== | ||
| - | 1QDM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Active as [http://en.wikipedia.org/wiki/Phytepsin Phytepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.40 3.4.23.40] Full crystallographic information is available from [http:// | + | 1QDM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Active as [http://en.wikipedia.org/wiki/Phytepsin Phytepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.40 3.4.23.40] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QDM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Costa, J.]] | [[Category: Costa, J.]] | ||
[[Category: Kervinen, J.]] | [[Category: Kervinen, J.]] | ||
| - | [[Category: Tobin, G | + | [[Category: Tobin, G J.]] |
| - | [[Category: Waugh, D | + | [[Category: Waugh, D S.]] |
[[Category: Wlodawer, A.]] | [[Category: Wlodawer, A.]] | ||
[[Category: Zdanov, A.]] | [[Category: Zdanov, A.]] | ||
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[[Category: zymogen structure]] | [[Category: zymogen structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:38:32 2008'' |
Revision as of 12:38, 21 February 2008
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CRYSTAL STRUCTURE OF PROPHYTEPSIN, A ZYMOGEN OF A BARLEY VACUOLAR ASPARTIC PROTEINASE.
Overview
We determined at 2.3 A resolution the crystal structure of prophytepsin, a zymogen of a barley vacuolar aspartic proteinase. In addition to the classical pepsin-like bilobal main body of phytepsin, we also traced most of the propeptide, as well as an independent plant-specific domain, never before described in structural terms. The structure revealed that, in addition to the propeptide, 13 N-terminal residues of the mature phytepsin are essential for inactivation of the enzyme. Comparison of the plant-specific domain with NK-lysin indicates that these two saposin-like structures are closely related, suggesting that all saposins and saposin-like domains share a common topology. Structural analysis of prophytepsin led to the identification of a putative membrane receptor-binding site involved in Golgi-mediated transport to vacuoles.
About this Structure
1QDM is a Single protein structure of sequence from Hordeum vulgare. Active as Phytepsin, with EC number 3.4.23.40 Full crystallographic information is available from OCA.
Reference
Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting., Kervinen J, Tobin GJ, Costa J, Waugh DS, Wlodawer A, Zdanov A, EMBO J. 1999 Jul 15;18(14):3947-55. PMID:10406799
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