1qdm: Difference between revisions
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[[Image:1qdm.gif|left|200px]] | [[Image:1qdm.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF PROPHYTEPSIN, A ZYMOGEN OF A BARLEY VACUOLAR ASPARTIC PROTEINASE.''' | {{Structure | ||
|PDB= 1qdm |SIZE=350|CAPTION= <scene name='initialview01'>1qdm</scene>, resolution 2.3Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF PROPHYTEPSIN, A ZYMOGEN OF A BARLEY VACUOLAR ASPARTIC PROTEINASE.''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1QDM is a [ | 1QDM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QDM OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10406799 10406799] | ||
[[Category: Hordeum vulgare]] | [[Category: Hordeum vulgare]] | ||
[[Category: Phytepsin]] | [[Category: Phytepsin]] | ||
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[[Category: Wlodawer, A.]] | [[Category: Wlodawer, A.]] | ||
[[Category: Zdanov, A.]] | [[Category: Zdanov, A.]] | ||
[[Category: aspartic | [[Category: aspartic proteinase]] | ||
[[Category: phytepsin]] | [[Category: phytepsin]] | ||
[[Category: saposin-like domain]] | [[Category: saposin-like domain]] | ||
[[Category: zymogen structure]] | [[Category: zymogen structure]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:36:12 2008'' | ||
Revision as of 14:36, 20 March 2008
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| , resolution 2.3Å | |||||||
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| Activity: | Phytepsin, with EC number 3.4.23.40 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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