View source for 5owf


==Structure of a LAO-binding protein mutant with glutamine==
<StructureSection load='5owf' size='340' side='right'caption='[[5owf]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5owf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OWF 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]] 1.91&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLN:GLUTAMINE'>GLN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=5owf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5owf OCA], [https://pdbe.org/5owf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5owf RCSB], [https://www.ebi.ac.uk/pdbsum/5owf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5owf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ARGT_SALTY ARGT_SALTY] This periplasmic binding protein is involved in an arginine transport system. ArgT and histidine-binding protein J (HisJ) interact with a common membrane-bound receptor, HisP.
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== Publication Abstract from PubMed ==
Computational protein design is still a challenge for advancing structure-function relationships. While recent advances in this field are promising, more information for genuine predictions is needed. Here, we discuss different approaches applied to install novel glutamine (Gln) binding into the Lysine/Arginine/Ornithine binding protein (LAOBP) from Salmonella typhimurium. We studied the ligand binding behaviour of two mutants: a binding pocket grafting design based on a structural superposition of LAOBP to the Gln binding protein QBP from Escherichia coli and a design based on statistical coupled positions. The latter showed the ability to bind Gln even though the protein was not very stable. Comparison of both approaches highlighted a non-conservative shared point mutation between LAOBP_graft and LAOBP_sca. This context dependent L117K mutation in LAOBP turned out to be sufficient for introducing Gln binding, as confirmed by different experimental techniques. Moreover, the crystal structure of LAOBP_L117K in complex with its ligand is reported. This article is protected by copyright. All rights reserved.

Redesign of LAOBP to bind novel L-amino acid ligands.,Banda-Vazquez J, Shanmugaratnam S, Rodriguez-Sotres R, Torres-Larios A, Hocker B, Sosa-Peinado A Protein Sci. 2018 Mar 10. doi: 10.1002/pro.3403. PMID:29524280<ref>PMID:29524280</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5owf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]]
[[Category: Banda-Vazquez J]]
[[Category: Hocker B]]
[[Category: Shanmugaratnam S]]
[[Category: Sosa-Peinado A]]