7ntg: Difference between revisions
New page: '''Unreleased structure''' The entry 7ntg is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==Bdellovibrio bacteriovorus PGI in complex with fructose-6-phosphate== | ||
<StructureSection load='7ntg' size='340' side='right'caption='[[7ntg]], [[Resolution|resolution]] 1.67Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7ntg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bdellovibrio_bacteriovorus_HD100 Bdellovibrio bacteriovorus HD100]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NTG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NTG 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]] 1.67Å</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=F6R:FRUCTOSE+-6-PHOSPHATE'>F6R</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=7ntg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ntg OCA], [https://pdbe.org/7ntg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ntg RCSB], [https://www.ebi.ac.uk/pdbsum/7ntg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ntg ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6MPU9_BDEBA Q6MPU9_BDEBA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Glycolysis and gluconeogenesis are central pathways of metabolism across all domains of life. A prominent enzyme in these pathways is phosphoglucose isomerase (PGI), which mediates the interconversion of glucose-6-phosphate and fructose-6-phosphate. The predatory bacterium Bdellovibrio bacteriovorus leads a complex life cycle, switching between intraperiplasmic replicative and extracellular 'hunter' attack-phase stages. Passage through this complex life cycle involves different metabolic states. Here we present the unliganded and substrate-bound structures of the B. bacteriovorus PGI, solved to 1.74 A and 1.67 A, respectively. These structures reveal that an induced-fit conformational change within the active site is not a prerequisite for the binding of substrates in some PGIs. Crucially, we suggest a phenylalanine residue, conserved across most PGI enzymes but substituted for glycine in B. bacteriovorus and other select organisms, is central to the induced-fit mode of substrate recognition for PGIs. This enzyme also represents the smallest conventional PGI characterized to date and probably represents the minimal requirements for a functional PGI. | |||
Bdellovibrio bacteriovorus phosphoglucose isomerase structures reveal novel rigidity in the active site of a selected subset of enzymes upon substrate binding.,Meek RW, Cadby IT, Lovering AL Open Biol. 2021 Aug;11(8):210098. doi: 10.1098/rsob.210098. Epub 2021 Aug 11. PMID:34375548<ref>PMID:34375548</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7ntg" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Phosphoglucose isomerase 3D structures|Phosphoglucose isomerase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bdellovibrio bacteriovorus HD100]] | |||
[[Category: Large Structures]] | |||
[[Category: Lovering AL]] | |||
[[Category: Meek RW]] | |||
Latest revision as of 15:39, 1 February 2024
Bdellovibrio bacteriovorus PGI in complex with fructose-6-phosphateBdellovibrio bacteriovorus PGI in complex with fructose-6-phosphate
Structural highlights
FunctionPublication Abstract from PubMedGlycolysis and gluconeogenesis are central pathways of metabolism across all domains of life. A prominent enzyme in these pathways is phosphoglucose isomerase (PGI), which mediates the interconversion of glucose-6-phosphate and fructose-6-phosphate. The predatory bacterium Bdellovibrio bacteriovorus leads a complex life cycle, switching between intraperiplasmic replicative and extracellular 'hunter' attack-phase stages. Passage through this complex life cycle involves different metabolic states. Here we present the unliganded and substrate-bound structures of the B. bacteriovorus PGI, solved to 1.74 A and 1.67 A, respectively. These structures reveal that an induced-fit conformational change within the active site is not a prerequisite for the binding of substrates in some PGIs. Crucially, we suggest a phenylalanine residue, conserved across most PGI enzymes but substituted for glycine in B. bacteriovorus and other select organisms, is central to the induced-fit mode of substrate recognition for PGIs. This enzyme also represents the smallest conventional PGI characterized to date and probably represents the minimal requirements for a functional PGI. Bdellovibrio bacteriovorus phosphoglucose isomerase structures reveal novel rigidity in the active site of a selected subset of enzymes upon substrate binding.,Meek RW, Cadby IT, Lovering AL Open Biol. 2021 Aug;11(8):210098. doi: 10.1098/rsob.210098. Epub 2021 Aug 11. PMID:34375548[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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