View source for 3wwm


==Crystal structure of LysZ from Thermus thermophilus with ADP==
<StructureSection load='3wwm' size='340' side='right'caption='[[3wwm]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wwm]] 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=3WWM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WWM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></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=3wwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wwm OCA], [https://pdbe.org/3wwm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wwm RCSB], [https://www.ebi.ac.uk/pdbsum/3wwm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wwm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LYSZ_THET2 LYSZ_THET2] Catalyzes the phosphorylation of LysW-gamma-alpha-aminoadipate. Does not phosphorylate N-acetyl-glutamate.<ref>PMID:25392000</ref> 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:25392000</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wwm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus thermophilus HB27]]
[[Category: Kuzuyama T]]
[[Category: Nishiyama M]]
[[Category: Tomita T]]
[[Category: Yoshida A]]