View source for 5zjg


==Gamma-glutamyltranspeptidase from Pseudomonas nitroreducens complexed with Gly-Gly==
<StructureSection load='5zjg' size='340' side='right'caption='[[5zjg]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zjg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_nitroreducens Pseudomonas nitroreducens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZJG 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]] 1.702&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5zjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zjg OCA], [https://pdbe.org/5zjg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zjg RCSB], [https://www.ebi.ac.uk/pdbsum/5zjg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zjg ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Theanine (gamma-glutamylethylamide) is an amino acid analog that reduces blood pressure and improves immune responses. The Upsilon-glutamyltranspeptidase (GGT) from Pseudomonas nitroreducens IFO12694 (PnGGT) has a unique preference for primary amines as Upsilon-glutamyl acceptors over standard L-amino acids and peptides. This characteristic is useful for the synthesis of theanine. We used X-ray crystallographic analysis to understand the structural basis of PnGGT's hydrolysis and transpeptidation reactions and to characterize its previously unidentified acceptor site. Structural studies of PnGGT have shown that key interactions between three residues (Trp385, Phe417, and Trp525) distinguish PnGGT from other GGTs. We studied the roles of these residues in the distinct biochemical properties of PnGGT using site-directed mutagenesis. All mutants showed a significant decrease in hydrolysis activity and an increase in transpeptidase activity, suggesting that the aromatic side chains of Trp385, Phe417, and Trp525 were involved in the recognition of acceptor substrates. Abbreviations: Upsilon-glutamyl peptide, theanine, X-ray crystallography.

Crystal structure analysis and enzymatic characterization of gamma-glutamyltranspeptidase from Pseudomonas nitroreducens.,Hibi T, Imaoka M, Shimizu Y, Itoh T, Wakayama M Biosci Biotechnol Biochem. 2018 Dec 3:1-8. doi: 10.1080/09168451.2018.1547104. PMID:30507352<ref>PMID:30507352</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5zjg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas nitroreducens]]
[[Category: Hibi T]]
[[Category: Imaoka M]]
[[Category: Itoh T]]
[[Category: Wakayama M]]