7cf8: Difference between revisions
New page: '''Unreleased structure''' The entry 7cf8 is ON HOLD until Paper Publication Authors: Li, J., Gao, B., Ji, R. Description: PfkB(Mycobacterium marinum) [[Category: Unreleased Structures... |
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==PfkB(Mycobacterium marinum)== | |||
<StructureSection load='7cf8' size='340' side='right'caption='[[7cf8]], [[Resolution|resolution]] 2.21Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7cf8]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_marinum_M Mycobacterium marinum M]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21Å</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='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> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B2HEF4_MYCMM B2HEF4_MYCMM] | |||
<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> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7cf8" style="background-color:#fffaf0;"></div> | ||
[[Category: Ji | |||
[[Category: | ==See Also== | ||
*[[Fructokinase|Fructokinase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycobacterium marinum M]] | |||
[[Category: Gao B]] | |||
[[Category: Ji R]] | |||
[[Category: Li J]] | |||
Latest revision as of 19:07, 29 November 2023
PfkB(Mycobacterium marinum)PfkB(Mycobacterium marinum)
Structural highlights
FunctionPublication 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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