1qdm: Difference between revisions
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|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] | |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> | ||
|GENE= | |GENE= | ||
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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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[[Category: zymogen structure]] | [[Category: zymogen structure]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:12:16 2008'' | ||
Revision as of 23:12, 30 March 2008
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| , resolution 2.3Å | |||||||
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| Activity: | Phytepsin, with EC number 3.4.23.40 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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