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==Bdellovibrio bacteriovorus PGI in P3121 spacegroup== | ==Bdellovibrio bacteriovorus PGI in P3121 spacegroup== | ||
<StructureSection load='7nss' size='340' side='right'caption='[[7nss]]' scene=''> | <StructureSection load='7nss' size='340' side='right'caption='[[7nss]], [[Resolution|resolution]] 1.84Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NSS FirstGlance]. <br> | <table><tr><td colspan='2'>[[7nss]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bdeba Bdeba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NSS FirstGlance]. <br> | ||
</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=7nss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nss OCA], [https://pdbe.org/7nss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nss RCSB], [https://www.ebi.ac.uk/pdbsum/7nss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nss ProSAT]</span></td></tr> | </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></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pgi, Bd0741 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=264462 BDEBA])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] </span></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=7nss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nss OCA], [https://pdbe.org/7nss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nss RCSB], [https://www.ebi.ac.uk/pdbsum/7nss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nss ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<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> | |||
</div> | |||
<div class="pdbe-citations 7nss" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bdeba]] | |||
[[Category: Glucose-6-phosphate isomerase]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Lovering | [[Category: Lovering, A L]] | ||
[[Category: Meek | [[Category: Meek, R W]] | ||
[[Category: Glucose-6-phosphate isomerase isomerase phosphoglucose isomerase]] | |||
[[Category: Isomerase]] | |||
Revision as of 08:55, 6 October 2021
Bdellovibrio bacteriovorus PGI in P3121 spacegroupBdellovibrio bacteriovorus PGI in P3121 spacegroup
Structural highlights
Publication 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. References
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