8e1u: Difference between revisions
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==Propionibacterium freudenreichii PPi-dependent PEPCK in complex with malate== | |||
<StructureSection load='8e1u' size='340' side='right'caption='[[8e1u]], [[Resolution|resolution]] 2.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8e1u]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8E1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8E1U FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MLT:D-MALATE'>MLT</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=8e1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8e1u OCA], [https://pdbe.org/8e1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8e1u RCSB], [https://www.ebi.ac.uk/pdbsum/8e1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8e1u ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A160VN62_PROFR A0A160VN62_PROFR] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Phosphoenolpyruvate carboxykinases (PEPCK) are a well-studied family of enzymes responsible for the regulation of TCA cycle flux, where they catalyze the interconversion of oxaloacetic acid (OAA) and phosphoenolpyruvate (PEP) using a phosphoryl donor/acceptor. These enzymes have typically been divided into two nucleotide-dependent classes, those that use ATP and those that use GTP. In the 1960's and early 1970's, a group of papers detailed biochemical properties of an enzyme named phosphoenolpyruvate carboxytransphosphorylase (later identified as a third PEPCK) from Propionibacterium freudenreichii (PP(i) -PfPEPCK), which instead of using a nucleotide, utilized PP(i) to catalyze the same interconversion of OAA and PEP. The presented work expands upon the initial biochemical experiments for PP(i) -PfPEPCK and interprets these data considering both the current understanding of nucleotide-dependent PEPCKs and is supplemented with a new crystal structure of PP(i) -PfPEPCK in complex with malate at a putative allosteric site. Most interesting, the data are consistent with PP(i) -PfPEPCK being a Fe(2+) activated enzyme in contrast with the Mn(2+) activated nucleotide-dependent enzymes which in part results in some unique kinetic properties for the enzyme when compared to the more widely distributed GTP- and ATP-dependent enzymes. | |||
Biochemical, structural, and kinetic characterization of PP(i) -dependent phosphoenolpyruvate carboxykinase from Propionibacterium freudenreichii.,McLeod MJ, Holyoak T Proteins. 2023 May 24. doi: 10.1002/prot.26513. PMID:37226637<ref>PMID:37226637</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Holyoak | <div class="pdbe-citations 8e1u" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Propionibacterium freudenreichii subsp. shermanii]] | |||
[[Category: Holyoak T]] | |||
[[Category: McLeod MJ]] | |||
Revision as of 05:39, 7 June 2023
Propionibacterium freudenreichii PPi-dependent PEPCK in complex with malate
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