This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1epo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:04, 20 March 2024) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1epo.jpg|left|200px]]
 
-
<!--
+
==ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN) COMPLEXED WITH CP-81,282 (MOR PHE NLE CHF NME)==
-
The line below this paragraph, containing "STRUCTURE_1epo", creates the "Structure Box" on the page.
+
<StructureSection load='1epo' size='340' side='right'caption='[[1epo]], [[Resolution|resolution]] 2.00&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'>[[1epo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryphonectria_parasitica Cryphonectria parasitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EPO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EPO 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&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2Z3:N-(MORPHOLIN-4-YLCARBONYL)-L-PHENYLALANYL-N-[(1R)-1-(CYCLOHEXYLMETHYL)-3,3-DIFLUORO-2,2-DIHYDROXY-4-(METHYLAMINO)-4-OXOBUTYL]-L-NORLEUCINAMIDE'>2Z3</scene></td></tr>
-
{{STRUCTURE_1epo| PDB=1epo | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1epo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1epo OCA], [https://pdbe.org/1epo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1epo RCSB], [https://www.ebi.ac.uk/pdbsum/1epo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1epo ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/CARP_CRYPA CARP_CRYPA]
 +
== 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/ep/1epo_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1epo ConSurf].
 +
<div style="clear:both"></div>
-
'''DIRECT OBSERVATION BY X-RAY ANALYSIS OF THE TETRAHEDRAL "INTERMEDIATE" OF ASPARTIC PROTEINASES'''
+
==See Also==
-
 
+
*[[Pepsin|Pepsin]]
-
 
+
*[[Proteinase 3D structures|Proteinase 3D structures]]
-
==Overview==
+
__TOC__
-
We report the X-ray analysis at 2.0 A resolution for crystals of the aspartic proteinase endothiapepsin (EC 3.4.23.6) complexed with a potent difluorostatone-containing tripeptide renin inhibitor (CP-81,282). The scissile bond surrogate, an electrophilic ketone, is hydrated in the complex. The pro-(R) (statine-like) hydroxyl of the tetrahedral carbonyl hydrate is hydrogen-bonded to both active-site aspartates 32 and 215 in the position occupied by a water in the native enzyme. The second hydroxyl oxygen of the hydrate is hydrogen-bonded only to the outer oxygen of Asp 32. These experimental data provide a basis for a model of the tetrahedral intermediate in aspartic proteinase-mediated cleavage of the amide bond. This indicates a mechanism in which Asp 32 is the proton donor and Asp 215 carboxylate polarizes a bound water for nucleophilic attack. The mechanism involves a carboxylate (Asp 32) that is stabilized by extensive hydrogen bonding, rather than an oxyanion derivative of the peptide as in serine proteinase catalysis.
+
</StructureSection>
-
 
+
[[Category: Cryphonectria parasitica]]
-
==About this Structure==
+
[[Category: Large Structures]]
-
1EPO is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EPO OCA].
+
[[Category: Blundell TL]]
-
 
+
[[Category: Cooper JB]]
-
==Reference==
+
[[Category: Veerapandian B]]
-
Direct observation by X-ray analysis of the tetrahedral "intermediate" of aspartic proteinases., Veerapandian B, Cooper JB, Sali A, Blundell TL, Rosati RL, Dominy BW, Damon DB, Hoover DJ, Protein Sci. 1992 Mar;1(3):322-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1304340 1304340]
+
-
[[Category: Endothiapepsin]]
+
-
[[Category: Single protein]]
+
-
[[Category: Blundell, T L.]]
+
-
[[Category: Cooper, J B.]]
+
-
[[Category: Veerapandian, B.]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:22:56 2008''
+

Current revision

ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN) COMPLEXED WITH CP-81,282 (MOR PHE NLE CHF NME)

PDB ID 1epo

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools