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| | <StructureSection load='2zp7' size='340' side='right'caption='[[2zp7]], [[Resolution|resolution]] 2.26Å' scene=''> | | <StructureSection load='2zp7' size='340' side='right'caption='[[2zp7]], [[Resolution|resolution]] 2.26Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2zp7]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thet2 Thet2]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2zg5 2zg5] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2dtv 2dtv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZP7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2zp7]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZP7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lysN ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/2-aminoadipate_transaminase 2-aminoadipate transaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.39 2.6.1.39] </span></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=2zp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zp7 OCA], [https://pdbe.org/2zp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zp7 RCSB], [https://www.ebi.ac.uk/pdbsum/2zp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zp7 ProSAT]</span></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=2zp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zp7 OCA], [https://pdbe.org/2zp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zp7 RCSB], [https://www.ebi.ac.uk/pdbsum/2zp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zp7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/LYSN_THET2 LYSN_THET2]] Catalyzes the transfer of an amino group between 2-oxoadipate (2-OA) and glutamate (Glu) to yield alpha-aminodipate (AAA). It can also transaminate glutamate, leucine, and aromatic amino acids. It also contributes in the biosynthesis of other amino acids such as leucine.<ref>PMID:15256574</ref>
| + | [https://www.uniprot.org/uniprot/LYSN_THET2 LYSN_THET2] Catalyzes the transfer of an amino group between 2-oxoadipate (2-OA) and glutamate (Glu) to yield alpha-aminodipate (AAA). It can also transaminate glutamate, leucine, and aromatic amino acids. It also contributes in the biosynthesis of other amino acids such as leucine.<ref>PMID:15256574</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zp/2zp7_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zp/2zp7_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 2-aminoadipate transaminase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thet2]] | + | [[Category: Thermus thermophilus HB27]] |
| - | [[Category: Fushinobu, S]] | + | [[Category: Fushinobu S]] |
| - | [[Category: Kuzuyama, T]] | + | [[Category: Kuzuyama T]] |
| - | [[Category: Miyagawa, T]] | + | [[Category: Miyagawa T]] |
| - | [[Category: Miyazaki, T]] | + | [[Category: Miyazaki T]] |
| - | [[Category: Nishiyama, M]] | + | [[Category: Nishiyama M]] |
| - | [[Category: Tomita, T]] | + | [[Category: Tomita T]] |
| - | [[Category: Alpha-aminoadipate aminotransferase]]
| + | |
| - | [[Category: Aminotransferase]]
| + | |
| - | [[Category: Plp-leucine complex]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
LYSN_THET2 Catalyzes the transfer of an amino group between 2-oxoadipate (2-OA) and glutamate (Glu) to yield alpha-aminodipate (AAA). It can also transaminate glutamate, leucine, and aromatic amino acids. It also contributes in the biosynthesis of other amino acids such as leucine.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
alpha-Aminoadipate aminotransferase (AAA-AT), a homolog of mammalian kynurenine aminotransferase II (Kat II), transfers an amino group to 2-oxoadipate to yield alpha-aminoadipate in lysine biosynthesis through the alpha-aminoadipate pathway in Thermus thermophilus. AAA-AT catalyzes transamination against various substrates, including AAA, glutamate, leucine, and aromatic amino acids. To elucidate the structural change for recognition of various substrates, we determined crystal structures of AAA-AT in four forms: with pyridoxal 5'-phosphate (PLP) (PLP complex), with PLP and leucine (PLP/Leu complex), with N-phosphopyridoxyl-leucine (PPL) (PPL complex), and with N-phosphopyridoxyl-alpha-aminoadipate (PPA) at 2.67, 2.26, 1.75, and 1.67 A resolution, respectively. The PLP complex is in an open state, whereas PLP/Leu, PPL, and PPA complexes are in closed states with maximal displacement (over 7 A) of the alpha2 helix and the beta1 strand in the small domain to cover the active site, indicating that conformational change is induced by substrate binding. In PPL and PLP/Leu complexes, several hydrophobic residues on the alpha2 helix recognize the hydrophobic side chain of the bound leucine moiety whereas, in the PPA complex, the alpha2 helix rotates to place the guanidium moiety of Arg23 on the helix at the appropriate position to interact with the carboxyl side chain of the AAA moiety. These results indicate that AAA-AT can recognize various kinds of substrates using the mobile alpha2 helix. The crystal structures and site-directed mutagenesis revealed that intersubunit-electrostatic interactions contribute to the elevated thermostability of this enzyme. Proteins 2008. (c) 2008 Wiley-Liss, Inc.
Mechanism for multiple-substrates recognition of alpha-aminoadipate aminotransferase from Thermus thermophilus.,Tomita T, Miyagawa T, Miyazaki T, Fushinobu S, Kuzuyama T, Nishiyama M Proteins. 2008 Sep 2. PMID:18831049[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Miyazaki T, Miyazaki J, Yamane H, Nishiyama M. alpha-Aminoadipate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus. Microbiology. 2004 Jul;150(Pt 7):2327-34. PMID:15256574 doi:10.1099/mic.0.27037-0
- ↑ Tomita T, Miyagawa T, Miyazaki T, Fushinobu S, Kuzuyama T, Nishiyama M. Mechanism for multiple-substrates recognition of alpha-aminoadipate aminotransferase from Thermus thermophilus. Proteins. 2008 Sep 2. PMID:18831049 doi:10.1002/prot.22245
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