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.


1arh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:32, 7 February 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1arh.gif|left|200px]]
 
-
{{Structure
+
==ASPARTATE AMINOTRANSFERASE, Y225R/R386A MUTANT==
-
|PDB= 1arh |SIZE=350|CAPTION= <scene name='initialview01'>1arh</scene>, resolution 2.3&Aring;
+
<StructureSection load='1arh' size='340' side='right'caption='[[1arh]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=PPD:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYLENE)-AMINO]-SUCCINIC ACID'>PPD</scene>
+
<table><tr><td colspan='2'>[[1arh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ARH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ARH FirstGlance]. <br>
-
|ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1]
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PPD:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYLENE)-AMINO]-SUCCINIC+ACID'>PPD</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=1arh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1arh OCA], [https://pdbe.org/1arh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1arh RCSB], [https://www.ebi.ac.uk/pdbsum/1arh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1arh ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/AAT_ECOLI AAT_ECOLI]
 +
== 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/ar/1arh_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=1arh ConSurf].
 +
<div style="clear:both"></div>
-
'''ASPARTATE AMINOTRANSFERASE, Y225R/R386A MUTANT'''
+
==See Also==
-
 
+
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
The electron distribution in the coenzyme-substrate adduct of aspartate aminotransferase was changed by replacing active-site Arg386 with alanine and introducing a new arginine residue nearby. [Y225R, R386A]Aspartate aminotransferase decarboxylates L-aspartate to L-alanine (kcat = 0.04 s-1), while its transaminase activity towards dicarboxylic amino acids is decreased by three orders of magnitude (kcat = 0.19 s-1). Molecular-dynamics simulations based on the crystal structure of the mutant enzyme suggest that a new hydrogen bond to the imine N atom of the pyridoxal-5'-phosphate- aspartate adduct and an altered electrostatic potential around its beta-carboxylate group underlie the 650,000-fold increase in the ratio of beta-decarboxylase/transaminase activity.
+
-
 
+
-
==About this Structure==
+
-
1ARH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ARH OCA].
+
-
 
+
-
==Reference==
+
-
Changing the reaction specificity of a pyridoxal-5'-phosphate-dependent enzyme., Graber R, Kasper P, Malashkevich VN, Sandmeier E, Berger P, Gehring H, Jansonius JN, Christen P, Eur J Biochem. 1995 Sep 1;232(2):686-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7556224 7556224]
+
-
[[Category: Aspartate transaminase]]
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Jansonius, J N.]]
+
[[Category: Jansonius JN]]
-
[[Category: Malashkevich, V N.]]
+
[[Category: Malashkevich VN]]
-
[[Category: PPD]]
+
-
[[Category: transferase (aminotransferase)]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:01:24 2008''
+

Current revision

ASPARTATE AMINOTRANSFERASE, Y225R/R386A MUTANT

PDB ID 1arh

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/1arh"
Personal tools