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| <StructureSection load='3wwl' size='340' side='right'caption='[[3wwl]], [[Resolution|resolution]] 1.20Å' scene=''> | | <StructureSection load='3wwl' size='340' side='right'caption='[[3wwl]], [[Resolution|resolution]] 1.20Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3wwl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet2 Thet2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WWL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WWL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wwl]] is a 1 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=3WWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WWL FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UN1:2-AMINOHEXANEDIOIC+ACID'>UN1</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.2Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wwm|3wwm]], [[3wwn|3wwn]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=R0K:(2~{S})-2-[[(4~{S})-4-azanyl-5-oxidanyl-5-oxidanylidene-pentanoyl]amino]hexanedioic+acid'>R0K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lysW, TTHA1908 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2])</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=3wwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wwl OCA], [https://pdbe.org/3wwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wwl RCSB], [https://www.ebi.ac.uk/pdbsum/3wwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wwl ProSAT]</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=3wwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wwl OCA], [http://pdbe.org/3wwl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wwl RCSB], [http://www.ebi.ac.uk/pdbsum/3wwl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wwl ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/LYSW_THET8 LYSW_THET8] Carrier protein that bears the covalently bound substrates for lysine biosynthesis; the bound alpha-aminoadipate (AAA) is sequentially converted to L-lysine.<ref>PMID:19620981</ref> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Thet2]] | + | [[Category: Thermus thermophilus HB27]] |
- | [[Category: Kuzuyama, T]] | + | [[Category: Kuzuyama T]] |
- | [[Category: Nishiyama, M]] | + | [[Category: Nishiyama M]] |
- | [[Category: Tomita, T]] | + | [[Category: Tomita T]] |
- | [[Category: Yoshida, A]] | + | [[Category: Yoshida A]] |
- | [[Category: Amino acid carrier protein]]
| + | |
- | [[Category: Metal binding protein]]
| + | |
- | [[Category: Zinc finger]]
| + | |
| Structural highlights
Function
LYSW_THET8 Carrier protein that bears the covalently bound substrates for lysine biosynthesis; the bound alpha-aminoadipate (AAA) is sequentially converted to L-lysine.[1]
Publication Abstract from PubMed
In the biosynthesis of lysine by Thermus thermophilus, the metabolite alpha-ketoglutarate is converted to the intermediate alpha-aminoadipate (AAA), which is protected by the 54-amino acid acidic protein LysW. In this study, we determined the crystal structure of LysZ from T. thermophilus (TtLysZ), an amino acid kinase that catalyzes the second step in the AAA to lysine conversion, which was in a complex with LysW at a resolution of 1.85 A. A crystal analysis coupled with isothermal titration calorimetry of the TtLysZ mutants for TtLysW revealed tight interactions between LysZ and the globular and C-terminal extension domains of the LysW protein, which were mainly attributed to electrostatic forces. These results provided structural evidence for LysW acting as a protecting molecule for the alpha-amino group of AAA and also as a carrier protein to guarantee better recognition by biosynthetic enzymes for the efficient biosynthesis of lysine.
Structural insight into amino group-carrier protein-mediated lysine biosynthesis: crystal structure of the LysZ.LysW complex from Thermus thermophilus.,Yoshida A, Tomita T, Fujimura T, Nishiyama C, Kuzuyama T, Nishiyama M J Biol Chem. 2015 Jan 2;290(1):435-47. doi: 10.1074/jbc.M114.595983. Epub 2014, Nov 12. PMID:25392000[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Horie A, Tomita T, Saiki A, Kono H, Taka H, Mineki R, Fujimura T, Nishiyama C, Kuzuyama T, Nishiyama M. Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus. Nat Chem Biol. 2009 Sep;5(9):673-9. doi: 10.1038/nchembio.198. Epub 2009 Jul 20. PMID:19620981 doi:http://dx.doi.org/10.1038/nchembio.198
- ↑ Yoshida A, Tomita T, Fujimura T, Nishiyama C, Kuzuyama T, Nishiyama M. Structural insight into amino group-carrier protein-mediated lysine biosynthesis: crystal structure of the LysZ.LysW complex from Thermus thermophilus. J Biol Chem. 2015 Jan 2;290(1):435-47. doi: 10.1074/jbc.M114.595983. Epub 2014, Nov 12. PMID:25392000 doi:http://dx.doi.org/10.1074/jbc.M114.595983
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