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==PfkB(Mycobacterium marinum)== | ==PfkB(Mycobacterium marinum)== | ||
<StructureSection load='7cf8' size='340' side='right'caption='[[7cf8]]' scene=''> | <StructureSection load='7cf8' size='340' side='right'caption='[[7cf8]], [[Resolution|resolution]] 2.21Å' 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=7CF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CF8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7cf8]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycmm Mycmm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CF8 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=7cf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cf8 OCA], [https://pdbe.org/7cf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cf8 RCSB], [https://www.ebi.ac.uk/pdbsum/7cf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cf8 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pfkB, MMAR_4574 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216594 MYCMM])</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=7cf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cf8 OCA], [https://pdbe.org/7cf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cf8 RCSB], [https://www.ebi.ac.uk/pdbsum/7cf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cf8 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Phosphofructokinase B (PfkB) belongs to the ribokinase family, which uses the phosphorylated sugar as substrate, and catalyzes fructose-6-phosphate into fructose-1,6-diphosphate. However, the structural basis of Mycobacterium marinum PfkB is not clear. Here, we found that the PfkB protein was monomeric in solution, which was different from most enzymes in this family. The crystal structure of PfkB protein from M. marinum was solved at a resolution of 2.21 A. The PfkB structure consists of two domains, a major three-layered alpha/beta/alpha sandwich-like domain characteristic of the ribokinase-like superfamily, and a second domain composed of four-stranded beta sheets. Structural comparison analysis suggested that residues G236, A237, G238, and D239 could be critical for ATP catalysis and substrate binding of PfkB. Our current work provides new insights into understanding the mechanism of the glycolysis in M. marinum. | |||
Structural analysis and functional study of phosphofructokinase B (PfkB) from Mycobacterium marinum.,Gao B, Ji R, Li Z, Su X, Li H, Sun Y, Ji C, Gan J, Li J Biochem Biophys Res Commun. 2021 Nov 19;579:129-135. doi:, 10.1016/j.bbrc.2021.09.051. Epub 2021 Sep 23. PMID:34597996<ref>PMID:34597996</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7cf8" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Fructokinase|Fructokinase]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gao B]] | [[Category: Mycmm]] | ||
[[Category: Ji R]] | [[Category: Gao, B]] | ||
[[Category: Li J]] | [[Category: Ji, R]] | ||
[[Category: Li, J]] | |||
[[Category: Hydrolase]] | |||
[[Category: Kinase]] | |||
[[Category: Momer]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Pfkb]] | |||
[[Category: Sandwich]] | |||
Revision as of 13:03, 12 January 2022
PfkB(Mycobacterium marinum)PfkB(Mycobacterium marinum)
Structural highlights
Publication Abstract from PubMedPhosphofructokinase B (PfkB) belongs to the ribokinase family, which uses the phosphorylated sugar as substrate, and catalyzes fructose-6-phosphate into fructose-1,6-diphosphate. However, the structural basis of Mycobacterium marinum PfkB is not clear. Here, we found that the PfkB protein was monomeric in solution, which was different from most enzymes in this family. The crystal structure of PfkB protein from M. marinum was solved at a resolution of 2.21 A. The PfkB structure consists of two domains, a major three-layered alpha/beta/alpha sandwich-like domain characteristic of the ribokinase-like superfamily, and a second domain composed of four-stranded beta sheets. Structural comparison analysis suggested that residues G236, A237, G238, and D239 could be critical for ATP catalysis and substrate binding of PfkB. Our current work provides new insights into understanding the mechanism of the glycolysis in M. marinum. Structural analysis and functional study of phosphofructokinase B (PfkB) from Mycobacterium marinum.,Gao B, Ji R, Li Z, Su X, Li H, Sun Y, Ji C, Gan J, Li J Biochem Biophys Res Commun. 2021 Nov 19;579:129-135. doi:, 10.1016/j.bbrc.2021.09.051. Epub 2021 Sep 23. PMID:34597996[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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