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.


1ane

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1ane" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ane, resolution 2.2&Aring;" /> '''ANIONIC TRYPSIN WILD ...)
Current revision (15:26, 13 March 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1ane.jpg|left|200px]]<br /><applet load="1ane" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1ane, resolution 2.2&Aring;" />
 
-
'''ANIONIC TRYPSIN WILD TYPE'''<br />
 
-
==Overview==
+
==ANIONIC TRYPSIN WILD TYPE==
-
The X-ray crystal structure of the copper complex of the rat trypsin, mutant Arg96 to His96 (trypsin R96H) has been determined in order to, ascertain the nature of the engineered metal-binding site and to, understand the structural basis for the metal-induced enzymatic, inhibition. In the structure, the catalytically essential His57 residue is, reoriented out of the active-site pocket and forms a chelating, metal-binding site with residue His96. The copper is bound to the N, epsilon 2 atoms of both histidine residues with Cu-N epsilon 2 = 2.2 A and, N epsilon 2-Cu-N epsilon 2 = 89 degrees. The metal is clearly bound to a, third ligand leading to a distorted square planar geometry at Cu. The, X-ray results do not unambiguously yield the identity of this third, ligand, but chemical data suggest that it is a deprotonated, chelating, Tris molecule which was used as a carrier to solubilize the copper in, alkaline solution (pH 8.0). Upon reorientation of His57, a unique water, molecule moves into the active site and engages in hydrogen-bonding with, Asp102-O delta 2 and His57-N delta 1. Except for small movements of the, peptide backbone near His96, the remainder of the trypsin molecule is, isostructural with the native enzyme. These data support the notion that, the effective inhibition of catalytic activity by metal ions observed in, trypsin R96H is indeed caused by a specific and reversible reorganization, of the active site in the enzyme.
+
<StructureSection load='1ane' size='340' side='right'caption='[[1ane]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1ane]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ANE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ANE 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]] 2.2&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</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=1ane FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ane OCA], [https://pdbe.org/1ane PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ane RCSB], [https://www.ebi.ac.uk/pdbsum/1ane PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ane ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/TRY2_RAT TRY2_RAT]
 +
== 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/an/1ane_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=1ane ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1ANE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] with BEN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ANE OCA].
+
*[[Trypsin 3D structures|Trypsin 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Structure of an engineered, metal-actuated switch in trypsin., McGrath ME, Haymore BL, Summers NL, Craik CS, Fletterick RJ, Biochemistry. 1993 Mar 2;32(8):1914-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8448149 8448149]
+
[[Category: Large Structures]]
[[Category: Rattus rattus]]
[[Category: Rattus rattus]]
-
[[Category: Single protein]]
+
[[Category: Fletterick RJ]]
-
[[Category: Trypsin]]
+
[[Category: Mcgrath ME]]
-
[[Category: Fletterick, R.J.]]
+
-
[[Category: Mcgrath, M.E.]]
+
-
[[Category: BEN]]
+
-
[[Category: anionic]]
+
-
[[Category: hydrolase]]
+
-
[[Category: serine protease]]
+
-
[[Category: trypsin]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:58:59 2007''
+

Current revision

ANIONIC TRYPSIN WILD TYPE

PDB ID 1ane

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ane"
Personal tools