View source for 8hnj


==Domain-stabilized glutamine-binding protein==
<StructureSection load='8hnj' size='340' side='right'caption='[[8hnj]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8hnj]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_908519 Escherichia coli 908519]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HNJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HNJ 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]] 2.03&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLN:GLUTAMINE'>GLN</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=8hnj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hnj OCA], [https://pdbe.org/8hnj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hnj RCSB], [https://www.ebi.ac.uk/pdbsum/8hnj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hnj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLNH_ECOLI GLNH_ECOLI] Involved in a glutamine-transport system GlnHPQ.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Stability is critical for the proper functioning of all proteins. Optimization of protein thermostability is a key step in the development of industrial enzymes and biologics. Herein, we demonstrate that multidomain proteins can be stabilized significantly using domain-based engineering followed by the recombination of the optimized domains. Domain-level analysis of designed protein variants with similar structures but different thermal profiles showed that the independent enhancement of the thermostability of a constituent domain improves the overall stability of the whole multidomain protein. The crystal structure and AlphaFold-predicted model of the designed proteins via domain-recombination provided a molecular explanation for domain-based stepwise stabilization. Our study suggests that domain-based modular engineering can minimize the sequence space for calculations in computational design and experimental errors, thereby offering useful guidance for multidomain protein engineering.

Domain-wise dissection of thermal stability enhancement in multidomain proteins.,Oh J, Durai P, Kannan P, Park J, Yeon YJ, Lee WK, Park K, Seo MH Int J Biol Macromol. 2023 May 15;237:124141. doi: 10.1016/j.ijbiomac.2023.124141. , Epub 2023 Mar 21. PMID:36958447<ref>PMID:36958447</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8hnj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli 908519]]
[[Category: Large Structures]]
[[Category: Choi SH]]
[[Category: Lee WK]]
[[Category: Park JH]]
[[Category: Park KW]]
[[Category: Seo MH]]