6f35: Difference between revisions
m Protected "6f35" [edit=sysop:move=sysop] |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal structure of the aspartate aminotranferase from Rhizobium meliloti== | |||
<StructureSection load='6f35' size='340' side='right'caption='[[6f35]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6f35]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ensifer_meliloti Ensifer meliloti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F35 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F35 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aatB, R03291, SMc04386 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266834 Ensifer meliloti])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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='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=6f35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f35 OCA], [http://pdbe.org/6f35 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f35 RCSB], [http://www.ebi.ac.uk/pdbsum/6f35 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f35 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/AATB_RHIME AATB_RHIME]] Involved in symbiotic nitrogen fixation. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Alternative routes for the post-chorismate branch of the biosynthetic pathway leading to tyrosine exist, the 4-hydroxyphenylpyruvate or the arogenate route. The arogenate route involves the transamination of prephenate into arogenate. In a previous study, we found that, depending on the microorganisms possessing the arogenate route, three different aminotransferases evolved to perform prephenate transamination i.e. 1beta aspartate aminotransferase (1beta AAT), N-succinyl-l,l-diaminopimelate aminotransferase, and branched-chain aminotransferase. The present work aimed at identifying molecular determinant(s) of 1beta AAT prephenate aminotransferase (PAT) activity. To that purpose, we conducted X-ray crystal structure analysis of two PAT competent 1beta AAT from Arabidopsis thaliana and Rhizobium meliloti, and one PAT incompetent 1beta AAT from Rhizobium meliloti. This structural analysis supported by site directed mutagenesis, modelling and molecular dynamics simulations allowed us to identify a molecular determinant of PAT activity in the flexible N-terminal loop of 1beta AAT. Our data reveal that a Lys/Arg/Gln residue in position 12 in the sequence (numbering according to Thermus thermophilus 1beta AAT), present only in PAT competent enzymes, could interact with the 4-hydroxyl group of the prephenate substrate, and thus may have a central role in the acquisition of PAT activity by 1beta AAT. This article is protected by copyright. All rights reserved. | |||
Tyrosine metabolism: identification of a key residue in the acquisition of prephenate aminotransferase activity by 1beta aspartate aminotransferase.,Giustini C, Graindorge M, Cobessi D, Crouzy S, Robin A, Curien G, Matringe M FEBS J. 2019 Feb 16. doi: 10.1111/febs.14789. PMID:30771275<ref>PMID:30771275</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6f35" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aspartate transaminase]] | |||
[[Category: Ensifer meliloti]] | |||
[[Category: Large Structures]] | |||
[[Category: Cobessi, D]] | |||
[[Category: Giustini, C]] | [[Category: Giustini, C]] | ||
[[Category: Graindorge, M]] | [[Category: Graindorge, M]] | ||
[[Category: Matringe, M]] | [[Category: Matringe, M]] | ||
[[Category: Aspartate amino-transferase]] | |||
[[Category: Transferase]] | |||
Latest revision as of 09:10, 12 June 2019
Crystal structure of the aspartate aminotranferase from Rhizobium melilotiCrystal structure of the aspartate aminotranferase from Rhizobium meliloti
Structural highlights
Function[AATB_RHIME] Involved in symbiotic nitrogen fixation. Publication Abstract from PubMedAlternative routes for the post-chorismate branch of the biosynthetic pathway leading to tyrosine exist, the 4-hydroxyphenylpyruvate or the arogenate route. The arogenate route involves the transamination of prephenate into arogenate. In a previous study, we found that, depending on the microorganisms possessing the arogenate route, three different aminotransferases evolved to perform prephenate transamination i.e. 1beta aspartate aminotransferase (1beta AAT), N-succinyl-l,l-diaminopimelate aminotransferase, and branched-chain aminotransferase. The present work aimed at identifying molecular determinant(s) of 1beta AAT prephenate aminotransferase (PAT) activity. To that purpose, we conducted X-ray crystal structure analysis of two PAT competent 1beta AAT from Arabidopsis thaliana and Rhizobium meliloti, and one PAT incompetent 1beta AAT from Rhizobium meliloti. This structural analysis supported by site directed mutagenesis, modelling and molecular dynamics simulations allowed us to identify a molecular determinant of PAT activity in the flexible N-terminal loop of 1beta AAT. Our data reveal that a Lys/Arg/Gln residue in position 12 in the sequence (numbering according to Thermus thermophilus 1beta AAT), present only in PAT competent enzymes, could interact with the 4-hydroxyl group of the prephenate substrate, and thus may have a central role in the acquisition of PAT activity by 1beta AAT. This article is protected by copyright. All rights reserved. Tyrosine metabolism: identification of a key residue in the acquisition of prephenate aminotransferase activity by 1beta aspartate aminotransferase.,Giustini C, Graindorge M, Cobessi D, Crouzy S, Robin A, Curien G, Matringe M FEBS J. 2019 Feb 16. doi: 10.1111/febs.14789. PMID:30771275[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||