2egy

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[[Image:2egy.jpg|left|200px]]<br /><applet load="2egy" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2egy, resolution 2.67&Aring;" />
 
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'''Crystal structure of LysN, alpha-aminoadipate aminotransferase (substrate free form), from Thermus thermophilus HB27'''<br />
 
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==Overview==
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==Crystal structure of LysN, alpha-aminoadipate aminotransferase (substrate free form), from Thermus thermophilus HB27==
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The extremely thermophilic bacterium Thermus thermophilus HB27 synthesizes lysine through alpha-aminoadipate (AAA). In this study, a T. thermophilus gene encoding the enzyme that catalyses transamination of AAA was cloned as a mammalian kynurenine/AAA aminotransferase (Kat2) gene homologue. A T. thermophilus mutant with disruption of the Kat2 homologue required a longer lag phase for growth and showed slower growth in minimal medium. Furthermore, addition of AAA or lysine shortened the lag phase and improved the growth rate. The Kat2 homologue was therefore termed lysN. LysN recognizes not only 2-oxoadipate, an intermediate of lysine biosynthesis, but also 2-oxoisocaproate, 2-oxoisovalerate and 2-oxo-3-methylvalerate, intermediates of leucine, valine and isoleucine biosyntheses, respectively, along with oxaloacetate, a compound in the TCA cycle, as an amino acceptor. These results suggest multiple roles of LysN in several cellular metabolic pathways including lysine and branched-chain amino acid biosyntheses.
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<StructureSection load='2egy' size='340' side='right'caption='[[2egy]], [[Resolution|resolution]] 2.67&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2egy]] is a 4 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=2EGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EGY FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.67&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2egy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2egy OCA], [https://pdbe.org/2egy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2egy RCSB], [https://www.ebi.ac.uk/pdbsum/2egy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2egy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eg/2egy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2egy ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2EGY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/2-aminoadipate_transaminase 2-aminoadipate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.39 2.6.1.39] Known structural/functional Sites: <scene name='pdbsite=AC1:Plp+Binding+Site+For+Residue+A+400'>AC1</scene>, <scene name='pdbsite=AC2:Plp+Binding+Site+For+Residue+B+400'>AC2</scene>, <scene name='pdbsite=AC3:Plp+Binding+Site+For+Residue+C+400'>AC3</scene> and <scene name='pdbsite=AC4:Plp+Binding+Site+For+Residue+D+400'>AC4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EGY OCA].
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*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
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== References ==
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==Reference==
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<references/>
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alpha-Aminoadipate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus., Miyazaki T, Miyazaki J, Yamane H, Nishiyama M, Microbiology. 2004 Jul;150(Pt 7):2327-34. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15256574 15256574]
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__TOC__
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[[Category: 2-aminoadipate transaminase]]
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</StructureSection>
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Thermus thermophilus]]
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[[Category: Thermus thermophilus HB27]]
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[[Category: Fushinobu, S.]]
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[[Category: Fushinobu S]]
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[[Category: Kuzuyama, T.]]
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[[Category: Kuzuyama T]]
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[[Category: Miyagawa, T.]]
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[[Category: Miyagawa T]]
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[[Category: Miyazaki, T.]]
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[[Category: Miyazaki T]]
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[[Category: Nishiyama, M.]]
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[[Category: Nishiyama M]]
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[[Category: Tomita, T.]]
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[[Category: Tomita T]]
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[[Category: PLP]]
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[[Category: alpha-aminoadipate aminotransferase]]
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[[Category: substrate specificity]]
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[[Category: thermus thermophilus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Mar 14 09:42:10 2008''
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Current revision

Crystal structure of LysN, alpha-aminoadipate aminotransferase (substrate free form), from Thermus thermophilus HB27

PDB ID 2egy

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