1dp5: Difference between revisions

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<StructureSection load='1dp5' size='340' side='right'caption='[[1dp5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1dp5' size='340' side='right'caption='[[1dp5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1dp5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DP5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1dp5]] 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=1DP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DP5 FirstGlance]. <br>
</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></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Saccharopepsin Saccharopepsin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] </span></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></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=1dp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dp5 OCA], [https://pdbe.org/1dp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dp5 RCSB], [https://www.ebi.ac.uk/pdbsum/1dp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dp5 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=1dp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dp5 OCA], [https://pdbe.org/1dp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dp5 RCSB], [https://www.ebi.ac.uk/pdbsum/1dp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dp5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CARP_YEAST CARP_YEAST]] Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself. [[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.  
[https://www.uniprot.org/uniprot/CARP_YEAST CARP_YEAST] Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1dp5 ConSurf].
</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=1dp5 ConSurf].
<div style="clear:both"></div>
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1dp5" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Proteinase|Proteinase]]
*[[Proteinase 3D structures|Proteinase 3D structures]]
*[[Proteinase 3D structures|Proteinase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharopepsin]]
[[Category: Dunn BM]]
[[Category: Dunn, B M]]
[[Category: Guschina A]]
[[Category: Guschina, A]]
[[Category: Kay J]]
[[Category: Kay, J]]
[[Category: Lees WE]]
[[Category: Lees, W E]]
[[Category: Li M]]
[[Category: Li, M]]
[[Category: Phylip HL]]
[[Category: Phylip, H L]]
[[Category: Winther JR]]
[[Category: Winther, J R]]
[[Category: Wlodawer A]]
[[Category: Wlodawer, A]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Ia3 mutant]]
[[Category: Mmm]]
[[Category: Proteinase some]]

Revision as of 12:52, 20 March 2024

THE STRUCTURE OF PROTEINASE A COMPLEXED WITH A IA3 MUTANT INHIBITORTHE STRUCTURE OF PROTEINASE A COMPLEXED WITH A IA3 MUTANT INHIBITOR

Structural highlights

1dp5 is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CARP_YEAST Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself.

Evolutionary Conservation

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

See Also

1dp5, resolution 2.20Å

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OCA
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