1qdm

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[[Image:1qdm.gif|left|200px]]
[[Image:1qdm.gif|left|200px]]
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{{Structure
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|PDB= 1qdm |SIZE=350|CAPTION= <scene name='initialview01'>1qdm</scene>, resolution 2.3&Aring;
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The line below this paragraph, containing "STRUCTURE_1qdm", creates the "Structure Box" on the page.
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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{{STRUCTURE_1qdm| PDB=1qdm | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qdm OCA], [http://www.ebi.ac.uk/pdbsum/1qdm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qdm RCSB]</span>
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'''CRYSTAL STRUCTURE OF PROPHYTEPSIN, A ZYMOGEN OF A BARLEY VACUOLAR ASPARTIC PROTEINASE.'''
'''CRYSTAL STRUCTURE OF PROPHYTEPSIN, A ZYMOGEN OF A BARLEY VACUOLAR ASPARTIC PROTEINASE.'''
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[[Category: Wlodawer, A.]]
[[Category: Wlodawer, A.]]
[[Category: Zdanov, A.]]
[[Category: Zdanov, A.]]
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[[Category: aspartic proteinase]]
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[[Category: Aspartic proteinase]]
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[[Category: phytepsin]]
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[[Category: Phytepsin]]
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[[Category: saposin-like domain]]
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[[Category: Saposin-like domain]]
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[[Category: zymogen structure]]
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[[Category: Zymogen structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:09:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:12:16 2008''
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Revision as of 03:09, 3 May 2008

Image:1qdm.gif

Template:STRUCTURE 1qdm

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. 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 Page seeded by OCA on Sat May 3 06:09:49 2008

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