1qdm: Difference between revisions

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[[Image:1qdm.gif|left|200px]]
[[Image:1qdm.gif|left|200px]]


{{Structure
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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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|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.]]
[[Category: aspartic proteinase]]
[[Category: Aspartic proteinase]]
[[Category: phytepsin]]
[[Category: Phytepsin]]
[[Category: saposin-like domain]]
[[Category: Saposin-like domain]]
[[Category: zymogen structure]]
[[Category: Zymogen structure]]
 
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Revision as of 06:09, 3 May 2008

File:1qdm.gif

Template:STRUCTURE 1qdm

CRYSTAL STRUCTURE OF PROPHYTEPSIN, A ZYMOGEN OF A BARLEY VACUOLAR ASPARTIC PROTEINASE.


OverviewOverview

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 StructureAbout this Structure

1QDM is a Single protein structure of sequence from Hordeum vulgare. Full crystallographic information is available from OCA.

ReferenceReference

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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