1dp5: Difference between revisions

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-{{Seed}}
-[[Image:1dp5.png|left|200px]]
-<!--
+==THE STRUCTURE OF PROTEINASE A COMPLEXED WITH A IA3 MUTANT INHIBITOR==
-The line below this paragraph, containing "STRUCTURE_1dp5", creates the "Structure Box" on the page.
+<StructureSection load='1dp5' size='340' side='right'caption='[[1dp5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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='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>
-{{STRUCTURE_1dp5|  PDB=1dp5  |  SCENE=  }}
+<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>
+== 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.
+== 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/1dp5_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=1dp5 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 STRUCTURE OF PROTEINASE A COMPLEXED WITH A IA3 MUTANT INHIBITOR===
+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==
-The line below this paragraph, {{ABSTRACT_PUBMED_10655612}}, adds the Publication Abstract to the page
+*[[Proteinase 3D structures|Proteinase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 10655612 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_10655612}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-DP5 is a 2 chains structure of sequences from [http://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].
-==Reference==
-<ref group="xtra">PMID:10655612</ref><references group="xtra"/>
 [[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: Ia3 mutant]]
-[[Category: Mmm]]
-[[Category: Proteinase some]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 07:13:09 2009''