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| | ==Crystal structure of Enolase from Bacillus subtilis.== | | ==Crystal structure of Enolase from Bacillus subtilis.== |
| - | <StructureSection load='4a3r' size='340' side='right' caption='[[4a3r]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='4a3r' size='340' side='right'caption='[[4a3r]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4a3r]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A3R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A3R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4a3r]] is a 4 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=4A3R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A3R FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a3s|4a3s]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] </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=4a3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a3r OCA], [https://pdbe.org/4a3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a3r RCSB], [https://www.ebi.ac.uk/pdbsum/4a3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a3r ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4a3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a3r OCA], [http://pdbe.org/4a3r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a3r RCSB], [http://www.ebi.ac.uk/pdbsum/4a3r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a3r ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ENO_BACSU ENO_BACSU]] Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.[HAMAP-Rule:MF_00318] | + | [https://www.uniprot.org/uniprot/ENO_BACSU ENO_BACSU] Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.[HAMAP-Rule:MF_00318] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Enolase|Enolase]] | + | *[[Enolase 3D structures|Enolase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus globigii migula 1900]] | + | [[Category: Bacillus subtilis]] |
| - | [[Category: Phosphopyruvate hydratase]] | + | [[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: Lyase]]
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| Structural highlights
Function
ENO_BACSU Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.[HAMAP-Rule:MF_00318]
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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