1qdm

From Proteopedia

(Difference between revisions)

Revision as of 09:54, 15 September 2021

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

Structural highlights

1qdm is a 3 chain structure with sequence from Hordeum vulgare. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Phytepsin, with EC number 3.4.23.40
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ASPR_HORVU] Involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kervinen J, Tobin GJ, Costa J, Waugh DS, Wlodawer A, Zdanov A. Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting. EMBO J. 1999 Jul 15;18(14):3947-55. PMID:10406799 doi:10.1093/emboj/18.14.3947

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='1qdm' size='340' side='right'caption='[[1qdm]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1qdm]] is a 3 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QDM FirstGlance]. <br>
+<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>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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>
+</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phytepsin Phytepsin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.40 3.4.23.40] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1qdm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qdm RCSB], [http://www.ebi.ac.uk/pdbsum/1qdm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qdm ProSAT]</span></td></tr>
+<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>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ASPR_HORVU ASPR_HORVU]] Involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles (By similarity).
+[[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]]

1qdm

From Proteopedia

Revision as of 09:54, 15 September 2021

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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