1akc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:31, 7 February 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1akc.gif|left|200px]]
 
-
{{Structure
+
==Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking its pyridoxal-5'-phosphate-binding lysine residue==
-
|PDB= 1akc |SIZE=350|CAPTION= <scene name='initialview01'>1akc</scene>, resolution 2.3&Aring;
+
<StructureSection load='1akc' size='340' side='right'caption='[[1akc]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=PPE:4-[(1,3-DICARBOXY-PROPYLAMINO)-METHYL]-3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDINIUM'>PPE</scene>
+
<table><tr><td colspan='2'>[[1akc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AKC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AKC FirstGlance]. <br>
-
|ACTIVITY= <span class='plainlinks'>[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] </span>
+
</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=PPE:4-[(1,3-DICARBOXY-PROPYLAMINO)-METHYL]-3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDINIUM'>PPE</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1akc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1akc OCA], [https://pdbe.org/1akc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1akc RCSB], [https://www.ebi.ac.uk/pdbsum/1akc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1akc ProSAT]</span></td></tr>
-
|RELATEDENTRY=
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1akc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1akc OCA], [http://www.ebi.ac.uk/pdbsum/1akc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1akc RCSB]</span>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/AATM_CHICK AATM_CHICK] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. May facilitate cellular uptake of long-chain free fatty acids (By similarity).
 +
== 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/ak/1akc_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=1akc ConSurf].
 +
<div style="clear:both"></div>
-
'''STRUCTURAL BASIS FOR THE CATALYTIC ACTIVITY OF ASPARTATE AMINOTRANSFERASE K258H LACKING ITS PYRIDOXAL-5'-PHOSPHATE-BINDING LYSINE RESIDUE'''
+
==See Also==
-
 
+
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
Chicken mitochondrial and Escherichia coli aspartate aminotransferases K258H, in which the active site lysine residue has been exchanged for a histidine residue, retain partial catalytic competence [Ziak et al. (1993) Eur. J. Biochem. 211, 475-484]. Mutant PLP and PMP holoenzymes and the complexes of the latter (E. coli enzyme) with sulfate and 2-oxoglutarate, as well as complexes of the mitochondrial apoenzyme with N-(5'-phosphopyridoxyl)-L-aspartate or N-(5'-phosphopyridoxyl)-L-glutamate, were crystallized and analyzed by means of X-ray crystallography in order to examine how the side chain of histidine 258 can substitute as a general acid/base catalyst of the aldimine-ketimine tautomerization in enzymic transamination. The structures have been solved and refined at resolutions between 2.1 and 2.8 A. Both the closed and the open conformations, identical to those of the wild-type enzyme, were observed, indicating that the mutant enzymes of both species exhibit the same conformational flexibility as the wild-type enzymes, although in AspAT K258H the equilibrium is somewhat shifted toward the open conformation. The replacement of the active site K258 by a histidine residue resulted only in local structural adaptations necessary to accommodate the imidazole ring. The catalytic competence of the mutant enzyme, which in the forward half-reaction is 0.1% of that of the wild-type enzyme, suggests that the imidazole group is involved in the aldimine-ketimine tautomerization. However, the imidazole ring of H258 is too far away from C alpha and C4' of the coenzyme-substrate adduct for direct proton transfer, suggesting that the 1,3-prototropic shift is mediated by a water molecule. Although there is enough space for a water molecule in this area, it has not been detected. Dynamic fluctuations of the protein matrix might transiently open a channel, giving a water molecule fleeting access to the active site.
+
-
 
+
-
==About this Structure==
+
-
1AKC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AKC OCA].
+
-
 
+
-
==Reference==
+
-
Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5'-phosphate-binding lysine residue., Malashkevich VN, Jager J, Ziak M, Sauder U, Gehring H, Christen P, Jansonius JN, Biochemistry. 1995 Jan 17;34(2):405-14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7819232 7819232]
+
-
[[Category: Aspartate transaminase]]
+
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Jansonius, J N.]]
+
[[Category: Jansonius JN]]
-
[[Category: Malashkevich, V N.]]
+
[[Category: Malashkevich VN]]
-
[[Category: transferase(aminotransferase)]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:42:04 2008''
+

Current revision

Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking its pyridoxal-5'-phosphate-binding lysine residue

PDB ID 1akc

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/1akc"
Personal tools