4l8l

</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=4l8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l8l OCA], [https://pdbe.org/4l8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l8l RCSB], [https://www.ebi.ac.uk/pdbsum/4l8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l8l ProSAT]</span></td></tr>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Pseudomonas aeruginosa causes opportunistic infections and is resistant to most antibiotics. Ongoing efforts to generate much-needed new antibiotics include targeting enzymes that are vital for P. aeruginosa but are absent in mammals. One such enzyme, type II dehydroquinase (DHQase), catalyzes the interconversion of 3-dehydroquinate and 3-dehydroshikimate, a necessary step in the shikimate pathway. This step is vital for the proper synthesis of phenylalanine, tryptophan, tyrosine and other aromatic metabolites. The recombinant expression, purification and crystal structure of catalytically active DHQase from P. aeruginosa (PaDHQase) are presented. Cubic crystals belonging to space group F23, with unit-cell parameters a = b = c = 125.39 A, were obtained by vapor diffusion in sitting drops and the structure was refined to an R factor of 16% at 1.74 A resolution. PaDHQase is a prototypical type II DHQase with the classical flavodoxin-like alpha/beta topology.

Structure of type II dehydroquinase from Pseudomonas aeruginosa.,Reiling S, Kelleher A, Matsumoto MM, Robinson G, Asojo OA Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1485-91. doi:, 10.1107/S2053230X14020214. Epub 2014 Oct 25. PMID:25372814<ref>PMID:25372814</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 4l8l" style="background-color:#fffaf0;"></div>

== References ==

<references/>