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1qdm

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

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Retrieved from "http://52.214.119.220/wiki/index.php/1qdm"

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-[[Image:1qdm.gif|left|200px]]
- {{Structure
+==CRYSTAL STRUCTURE OF PROPHYTEPSIN, A ZYMOGEN OF A BARLEY VACUOLAR ASPARTIC PROTEINASE.==
-|PDB= 1qdm |SIZE=350|CAPTION= <scene name='initialview01'>1qdm</scene>, resolution 2.3&Aring;
+<StructureSection load='1qdm' size='340' side='right'caption='[[1qdm]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<table><tr><td colspan='2'>[[1qdm]] is a 3 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QDM FirstGlance]. <br>
-|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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-|GENE=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qdm OCA], [https://pdbe.org/1qdm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qdm RCSB], [https://www.ebi.ac.uk/pdbsum/1qdm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qdm ProSAT]</span></td></tr>
-|DOMAIN=
+</table>
-|RELATEDENTRY=
+== Function ==
-|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>
+[https://www.uniprot.org/uniprot/ASPR_HORVU ASPR_HORVU] Involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles (By similarity).
-}}
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
-'''CRYSTAL STRUCTURE OF PROPHYTEPSIN, A ZYMOGEN OF A BARLEY VACUOLAR ASPARTIC PROTEINASE.'''
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qd/1qdm_consurf.spt"</scriptWhenChecked>
-==Overview==
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-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.
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
-==About this Structure==
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qdm ConSurf].
-QDM 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].
+<div style="clear:both"></div>
+__TOC__
-==Reference==
+</StructureSection>
-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: Phytepsin]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Costa J]]
-[[Category: Costa, J.]]
+[[Category: Kervinen J]]
-[[Category: Kervinen, J.]]
+[[Category: Tobin GJ]]
-[[Category: Tobin, G J.]]
+[[Category: Waugh DS]]
-[[Category: Waugh, D S.]]
+[[Category: Wlodawer A]]
-[[Category: Wlodawer, A.]]
+[[Category: Zdanov A]]
-[[Category: Zdanov, A.]]
-[[Category: aspartic proteinase]]
-[[Category: phytepsin]]
-[[Category: saposin-like domain]]
-[[Category: zymogen structure]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:12:16 2008''

1qdm

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

Structural highlights

Function

Evolutionary Conservation

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