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< | ==THE STRUCTURE OF PROTEINASE A COMPLEXED WITH IA3 PEPTIDE INHIBITOR== | ||
<StructureSection load='1dpj' size='340' side='right'caption='[[1dpj]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1dpj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DPJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DPJ FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1dpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpj OCA], [https://pdbe.org/1dpj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dpj RCSB], [https://www.ebi.ac.uk/pdbsum/1dpj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dpj ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/IPA3_YEAST IPA3_YEAST] Specific and potent inhibitor for yeast aspartic protease A (yscA). The proteinase acts as a folding template stabilizing the helical conformation in the inhibitor, which results in the potent and specific blockage of the proteolytic activity. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpj_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1dpj ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Aspartic proteinase A from yeast is specifically and potently inhibited by a small protein called IA3 from Saccharomyces cerevisiae. Although this inhibitor consists of 68 residues, we show that the inhibitory activity resides within the N-terminal half of the molecule. Structures solved at 2.2 and 1.8 A, respectively, for complexes of proteinase A with full-length IA3 and with a truncated form consisting only of residues 2-34, reveal an unprecedented mode of inhibitor-enzyme interactions. Neither form of the free inhibitor has detectable intrinsic secondary structure in solution. However, upon contact with the enzyme, residues 2-32 become ordered and adopt a near-perfect alpha-helical conformation. Thus, the proteinase acts as a folding template, stabilizing the helical conformation in the inhibitor, which results in the potent and specific blockage of the proteolytic activity. | |||
The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix.,Li M, Phylip LH, Lees WE, Winther JR, Dunn BM, Wlodawer A, Kay J, Gustchina A Nat Struct Biol. 2000 Feb;7(2):113-7. PMID:10655612<ref>PMID:10655612</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1dpj" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Proteinase 3D structures|Proteinase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
< | |||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Dunn BM]] | |||
[[Category: Dunn | [[Category: Guschina A]] | ||
[[Category: Guschina | [[Category: Kay J]] | ||
[[Category: Kay | [[Category: Lees WE]] | ||
[[Category: Lees | [[Category: Li M]] | ||
[[Category: Li | [[Category: Phylip HL]] | ||
[[Category: Phylip | [[Category: Winther JR]] | ||
[[Category: Winther | [[Category: Wlodawer A]] | ||
[[Category: Wlodawer | |||
Latest revision as of 02:54, 21 November 2024
THE STRUCTURE OF PROTEINASE A COMPLEXED WITH IA3 PEPTIDE INHIBITORTHE STRUCTURE OF PROTEINASE A COMPLEXED WITH IA3 PEPTIDE INHIBITOR
Structural highlights
FunctionIPA3_YEAST Specific and potent inhibitor for yeast aspartic protease A (yscA). The proteinase acts as a folding template stabilizing the helical conformation in the inhibitor, which results in the potent and specific blockage of the proteolytic activity. 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 PubMedAspartic proteinase A from yeast is specifically and potently inhibited by a small protein called IA3 from Saccharomyces cerevisiae. Although this inhibitor consists of 68 residues, we show that the inhibitory activity resides within the N-terminal half of the molecule. Structures solved at 2.2 and 1.8 A, respectively, for complexes of proteinase A with full-length IA3 and with a truncated form consisting only of residues 2-34, reveal an unprecedented mode of inhibitor-enzyme interactions. Neither form of the free inhibitor has detectable intrinsic secondary structure in solution. However, upon contact with the enzyme, residues 2-32 become ordered and adopt a near-perfect alpha-helical conformation. Thus, the proteinase acts as a folding template, stabilizing the helical conformation in the inhibitor, which results in the potent and specific blockage of the proteolytic activity. The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix.,Li M, Phylip LH, Lees WE, Winther JR, Dunn BM, Wlodawer A, Kay J, Gustchina A Nat Struct Biol. 2000 Feb;7(2):113-7. PMID:10655612[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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