4je5

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(Difference between revisions)

Revision as of 13:21, 5 August 2016

Crystal structure of the aromatic aminotransferase Aro8, a putative alpha-aminoadipate aminotransferase in Saccharomyces cerevisiae

Structural highlights

4je5 is a 4 chain structure with sequence from Baker's yeast. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
NonStd Res:
Gene:	ARO8, YGL202W (Baker's yeast)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ARO8_YEAST] General aromatic amino acid transaminase involved in several otherwise unrelated metabolic pathways. Responsible for phenylalanine and tyrosine biosynthesis. Active with glutamate, phenylalanine, tyrosine and tryptophan as amino donors and with phenylpyruvate, hydroxyphenylpyruvate, 2-oxoglutarate and pyruvate as amino acceptors. Also active with methionine, alpha-aminoadipate and leucine as amino donors when phenylpyruvate is the amino acceptor and in the reverse reactions with the corresponding oxo acids and phenylalanine as amino donor. Catalyzes the formation of methionine from 2-keto-4-methylthiobutyrate (KMTB) in the methionine salvage pathway primarily using aromatic amino acids (tyrosine, phenylalanine and tryptophan) as the amino donors. Catalyzes the formation of alpha-aminoadipate from alpha-ketoadipate in the lysine biosyntheic pathway.^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

alpha-Aminoadipate aminotransferase (AAA-AT) catalyzes the amination of 2-oxoadipate to alpha-aminoadipate in the fourth step of the alpha-aminoadipate pathway of lysine biosynthesis in fungi. The aromatic aminotransferase Aro8 has recently been identified as an AAA-AT in Saccharomyces cerevisiae. This enzyme displays broad substrate selectivity, utilizing several amino acids and 2-oxo acids as substrates. Here we report the 1.91A resolution crystal structure of Aro8 and compare it to AAA-AT LysN from Thermus thermophilus and human kynurenine aminotransferase II. Inspection of the active site of Aro8 reveals asymmetric cofactor binding with lysine-pyridoxal-5-phosphate bound within the active site of one subunit in the Aro8 homodimer and pyridoxamine phosphate and a HEPES molecule bound to the other subunit. The HEPES buffer molecule binds within the substrate-binding site of Aro8, yielding insights into the mechanism by which it recognizes multiple substrates and how this recognition differs from other AAA-AT/kynurenine aminotransferases.

Crystal structure of Saccharomyces cerevisiae Aro8, a putative alpha-aminoadipate aminotransferase.,Bulfer SL, Brunzelle JS, Trievel RC Protein Sci. 2013 Jul 24. doi: 10.1002/pro.2315. PMID:23893908^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Iraqui I, Vissers S, Cartiaux M, Urrestarazu A. Characterisation of Saccharomyces cerevisiae ARO8 and ARO9 genes encoding aromatic aminotransferases I and II reveals a new aminotransferase subfamily. Mol Gen Genet. 1998 Jan;257(2):238-48. PMID:9491083
↑ Kradolfer P, Niederberger P, Hutter R. Tryptophan degradation in Saccharomyces cerevisiae: characterization of two aromatic aminotransferases. Arch Microbiol. 1982 Dec 11;133(3):242-8. PMID:6763508
↑ Urrestarazu A, Vissers S, Iraqui I, Grenson M. Phenylalanine- and tyrosine-auxotrophic mutants of Saccharomyces cerevisiae impaired in transamination. Mol Gen Genet. 1998 Jan;257(2):230-7. PMID:9491082
↑ Pirkov I, Norbeck J, Gustafsson L, Albers E. A complete inventory of all enzymes in the eukaryotic methionine salvage pathway. FEBS J. 2008 Aug;275(16):4111-20. doi: 10.1111/j.1742-4658.2008.06552.x. Epub, 2008 Jul 10. PMID:18625006 doi:10.1111/j.1742-4658.2008.06552.x
↑ Karsten WE, Reyes ZL, Bobyk KD, Cook PF, Chooback L. Mechanism of the aromatic aminotransferase encoded by the Aro8 gene from Saccharomyces cerevisiae. Arch Biochem Biophys. 2011 Dec 1;516(1):67-74. doi: 10.1016/j.abb.2011.09.008., Epub 2011 Sep 29. PMID:21982920 doi:10.1016/j.abb.2011.09.008
↑ Bulfer SL, Brunzelle JS, Trievel RC. Crystal structure of Saccharomyces cerevisiae Aro8, a putative alpha-aminoadipate aminotransferase. Protein Sci. 2013 Jul 24. doi: 10.1002/pro.2315. PMID:23893908 doi:10.1002/pro.2315

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4je5"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the aromatic aminotransferase Aro8, a putative alpha-aminoadipate aminotransferase in Saccharomyces cerevisiae==
 <StructureSection load='4je5' size='340' side='right' caption='[[4je5]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4je5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JE5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JE5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4je5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JE5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JE5 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</scene></td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></td></tr>
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARO8, YGL202W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARO8, YGL202W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4je5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4je5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4je5 RCSB], [http://www.ebi.ac.uk/pdbsum/4je5 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4je5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4je5 OCA], [http://pdbe.org/4je5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4je5 RCSB], [http://www.ebi.ac.uk/pdbsum/4je5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4je5 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4je5" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Saccharomyces cerevisiae s288c]]
+[[Category: Baker's yeast]]
 [[Category: Brunzelle, J S]]
 [[Category: Bulfer, S L]]

4je5

From Proteopedia

Revision as of 13:21, 5 August 2016

Crystal structure of the aromatic aminotransferase Aro8, a putative alpha-aminoadipate aminotransferase in Saccharomyces cerevisiae

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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