9yrs: Difference between revisions
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New page: '''Unreleased structure''' The entry 9yrs is ON HOLD Authors: Andrews, J.R.W., Sakon, J., Fan, C. Description: E. Coli Glucokinase -K214Q Category: Unreleased Structures [[Category... |
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==E. Coli Glucokinase - K214Q== | |||
<StructureSection load='9yrs' size='340' side='right'caption='[[9yrs]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9yrs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9YRS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9YRS 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]] 2.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=9yrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9yrs OCA], [https://pdbe.org/9yrs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9yrs RCSB], [https://www.ebi.ac.uk/pdbsum/9yrs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9yrs ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/GLK_ECOLI GLK_ECOLI] Not highly important in E.coli as glucose is transported into the cell by the PTS system already as glucose 6-phosphate. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In this study, we report the crystal structures of K214Q and K216Q variants of Escherichia coli glucokinase (ecGLK), each of which is bound to phosphate in the active-site cleft. The structure of the K214Q variant was determined at 2.70 A resolution and refined with an R(work) and R(free) of 0.140 and 0.190, respectively, while that of the K216Q variant was determined at 2.44 A resolution with an R(work) and R(free) of 0.178 and 0.225, respectively. Both variants adopt an open conformation and maintain phosphate-binding interactions similar to the wild-type ecGLK. Structural comparison of the K214Q variant revealed large backbone deviations in the 214-224 alpha-helix, increased disorder in the loops surrounding the glucose-binding cleft and outward shifts of Asn99, Asp100, His160 and Glu187. Our previous study demonstrated that lysine acetylation at Lys214 and Lys216 impaired the activity of ecGLK, and here we show that acetylation mimics produced domain shifts, indicating those of lysine residues that could be essential for stabilizing the glucose-binding region of ecGLK. | |||
Crystal structures of Escherichia coli glucokinase acetylation-mimicking variants and insights into the impact of acetylation.,Andrews J, Sakon J, Fan C Acta Crystallogr F Struct Biol Commun. 2026 May 1;82(Pt 5):160-6. doi: , 10.1107/S2053230X26002803. PMID:41944126<ref>PMID:41944126</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 9yrs" style="background-color:#fffaf0;"></div> | ||
[[Category: Fan | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Andrews JRW]] | |||
[[Category: Fan C]] | |||
[[Category: Sakon J]] | |||
