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| | <StructureSection load='4a3s' size='340' side='right'caption='[[4a3s]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='4a3s' size='340' side='right'caption='[[4a3s]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4a3s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A3S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A3S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4a3s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A3S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A3S FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4a3r|4a3r]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/6-phosphofructokinase 6-phosphofructokinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.11 2.7.1.11] </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=4a3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a3s OCA], [https://pdbe.org/4a3s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a3s RCSB], [https://www.ebi.ac.uk/pdbsum/4a3s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a3s ProSAT]</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=4a3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a3s OCA], [https://pdbe.org/4a3s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a3s RCSB], [https://www.ebi.ac.uk/pdbsum/4a3s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a3s ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PFKA_BACSU PFKA_BACSU]] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.[HAMAP-Rule:MF_00339]
| + | [https://www.uniprot.org/uniprot/PFKA_BACSU PFKA_BACSU] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.[HAMAP-Rule:MF_00339] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| - | [[Category: 6-phosphofructokinase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Harwood, C R]] | + | [[Category: Harwood CR]] |
| - | [[Category: Hewitt, L]] | + | [[Category: Hewitt L]] |
| - | [[Category: Lewis, R J]] | + | [[Category: Lewis RJ]] |
| - | [[Category: Newman, J A]] | + | [[Category: Newman JA]] |
| - | [[Category: Rodrigues, C]] | + | [[Category: Rodrigues C]] |
| - | [[Category: Solovyova, A S]] | + | [[Category: Solovyova AS]] |
| - | [[Category: Degradosome]]
| + | |
| - | [[Category: Glycolysis]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
PFKA_BACSU Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.[HAMAP-Rule:MF_00339]
Publication Abstract from PubMed
The RNA degradosome is a multiprotein macromolecular complex that is involved in the degradation of messenger RNA in bacteria. The composition of this complex has been found to display a high degree of evolutionary divergence, which may reflect the adaptation of species to different environments. Recently, a degradosome-like complex identified in Bacillus subtilis was found to be distinct from those found in proteobacteria, the degradosomes of which are assembled around the unstructured C-terminus of ribonuclease E, a protein not present in B. subtilis. In this report, we have investigated in vitro the binary interactions between degradosome components and have characterized interactions between glycolytic enzymes, RNA-degrading enzymes, and those that appear to link these two cellular processes. The crystal structures of the glycolytic enzymes phosphofructokinase and enolase are presented and discussed in relation to their roles in the mediation of complex protein assemblies. Taken together, these data provide valuable insights into the structure and dynamics of the RNA degradosome, a fascinating and complex macromolecular assembly that links RNA degradation with central carbon metabolism.
Dissection of the network of interactions that links RNA processing with glycolysis in the Bacillus subtilis degradosome.,Newman JA, Hewitt L, Rodrigues C, Solovyova AS, Harwood CR, Lewis RJ J Mol Biol. 2012 Feb 10;416(1):121-36. Epub 2011 Dec 16. PMID:22198292[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Newman JA, Hewitt L, Rodrigues C, Solovyova AS, Harwood CR, Lewis RJ. Dissection of the network of interactions that links RNA processing with glycolysis in the Bacillus subtilis degradosome. J Mol Biol. 2012 Feb 10;416(1):121-36. Epub 2011 Dec 16. PMID:22198292 doi:10.1016/j.jmb.2011.12.024
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