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7nss
From Proteopedia
(Difference between revisions)
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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 05:55, 6 October 2021
Bdellovibrio bacteriovorus PGI in P3121 spacegroup
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