1dp5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1dp5" [edit=sysop:move=sysop])
Current revision (04:27, 17 October 2024) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
[[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]]
-
[[1dp5]] is a 2 chain structure with sequence 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: 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.]]
+

Current revision

THE STRUCTURE OF PROTEINASE A COMPLEXED WITH A IA3 MUTANT INHIBITOR

PDB ID 1dp5

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools