3h8a: Difference between revisions

Latest revision as of 07:17, 6 September 2023

Crystal structure of E. coli enolase bound to its cognate RNase E recognition domain

Structural highlights

3h8a is a 6 chain structure with sequence from Escherichia coli and Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:	MG
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ENO_ECOLI Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. It is also a component of the RNA degradosome, a multi-enzyme complex involved in RNA processing and messenger RNA degradation. Its interaction with RNase E is important for the turnover of mRNA, in particular on transcripts encoding enzymes of energy-generating metabolic routes. Its presence in the degradosome is required for the response to excess phosphosugar. May play a regulatory role in the degradation of specific RNAs, such as ptsG mRNA, therefore linking cellular metabolic status with post-translational gene regulation.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

In Escherichia coli and many other bacterial species, the glycolytic enzyme enolase is a component of the multi-enzyme RNA degradosome, an assembly that is involved in RNA processing and degradation. Enolase is recruited into the degradosome through interactions with a small recognition motif located within the degradosome-scaffolding domain of RNase E. Here, the crystal structure of enolase bound to its cognate site from RNase E (residues 823-850) at 1.9 A resolution is presented. The structure suggests that enolase may help to organize an adjacent conserved RNA-binding motif in RNase E.

Molecular recognition between Escherichia coli enolase and ribonuclease E.,Nurmohamed S, McKay AR, Robinson CV, Luisi BF Acta Crystallogr D Biol Crystallogr. 2010 Sep;66(Pt 9):1036-40. Epub 2010 Aug 13. PMID:20823555^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Py B, Higgins CF, Krisch HM, Carpousis AJ. A DEAD-box RNA helicase in the Escherichia coli RNA degradosome. Nature. 1996 May 9;381(6578):169-72. PMID:8610017 doi:https://dx.doi.org/10.1038/381169a0
↑ Bernstein JA, Lin PH, Cohen SN, Lin-Chao S. Global analysis of Escherichia coli RNA degradosome function using DNA microarrays. Proc Natl Acad Sci U S A. 2004 Mar 2;101(9):2758-63. Epub 2004 Feb 23. PMID:14981237 doi:https://dx.doi.org/10.1073/pnas.0308747101
↑ Morita T, Kawamoto H, Mizota T, Inada T, Aiba H. Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in Escherichia coli. Mol Microbiol. 2004 Nov;54(4):1063-75. PMID:15522087 doi:https://dx.doi.org/10.1111/j.1365-2958.2004.04329.x
↑ Nurmohamed S, McKay AR, Robinson CV, Luisi BF. Molecular recognition between Escherichia coli enolase and ribonuclease E. Acta Crystallogr D Biol Crystallogr. 2010 Sep;66(Pt 9):1036-40. Epub 2010 Aug 13. PMID:20823555 doi:10.1107/S0907444910030015

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Py B, Higgins CF, Krisch HM, Carpousis AJ. A DEAD-box RNA helicase in the Escherichia coli RNA degradosome. Nature. 1996 May 9;381(6578):169-72. PMID:8610017 doi:https://dx.doi.org/10.1038/381169a0

[2] Bernstein JA, Lin PH, Cohen SN, Lin-Chao S. Global analysis of Escherichia coli RNA degradosome function using DNA microarrays. Proc Natl Acad Sci U S A. 2004 Mar 2;101(9):2758-63. Epub 2004 Feb 23. PMID:14981237 doi:https://dx.doi.org/10.1073/pnas.0308747101

[3] Morita T, Kawamoto H, Mizota T, Inada T, Aiba H. Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in Escherichia coli. Mol Microbiol. 2004 Nov;54(4):1063-75. PMID:15522087 doi:https://dx.doi.org/10.1111/j.1365-2958.2004.04329.x

[4] Nurmohamed S, McKay AR, Robinson CV, Luisi BF. Molecular recognition between Escherichia coli enolase and ribonuclease E. Acta Crystallogr D Biol Crystallogr. 2010 Sep;66(Pt 9):1036-40. Epub 2010 Aug 13. PMID:20823555 doi:10.1107/S0907444910030015

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[3]

[4]

@@ Line 3: / Line 3: @@
 <StructureSection load='3h8a' size='340' side='right'caption='[[3h8a]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3h8a]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H8A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3H8A FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3h8a]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H8A 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></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]] 1.9&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3h8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h8a OCA], [http://pdbe.org/3h8a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3h8a RCSB], [http://www.ebi.ac.uk/pdbsum/3h8a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3h8a 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=3h8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h8a OCA], [https://pdbe.org/3h8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h8a RCSB], [https://www.ebi.ac.uk/pdbsum/3h8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h8a ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ENO_ECOLI ENO_ECOLI]] Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. It is also a component of the RNA degradosome, a multi-enzyme complex involved in RNA processing and messenger RNA degradation. Its interaction with RNase E is important for the turnover of mRNA, in particular on transcripts encoding enzymes of energy-generating metabolic routes. Its presence in the degradosome is required for the response to excess phosphosugar. May play a regulatory role in the degradation of specific RNAs, such as ptsG mRNA, therefore linking cellular metabolic status with post-translational gene regulation.<ref>PMID:8610017</ref> <ref>PMID:14981237</ref> <ref>PMID:15522087</ref>
+[https://www.uniprot.org/uniprot/ENO_ECOLI ENO_ECOLI] Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. It is also a component of the RNA degradosome, a multi-enzyme complex involved in RNA processing and messenger RNA degradation. Its interaction with RNase E is important for the turnover of mRNA, in particular on transcripts encoding enzymes of energy-generating metabolic routes. Its presence in the degradosome is required for the response to excess phosphosugar. May play a regulatory role in the degradation of specific RNAs, such as ptsG mRNA, therefore linking cellular metabolic status with post-translational gene regulation.<ref>PMID:8610017</ref> <ref>PMID:14981237</ref> <ref>PMID:15522087</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 33: @@
 *[[Enolase 3D structures|Enolase 3D structures]]
 *[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
-*[[Temp|Temp]]
 == References ==
 <references/>
@@ Line 39: / Line 38: @@
 </StructureSection>
 [[Category: Escherichia coli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Large Structures]]
-[[Category: Phosphopyruvate hydratase]]
+[[Category: Luisi BF]]
-[[Category: Luisi, B F]]
+[[Category: Nurmohamed S]]
-[[Category: Nurmohamed, S]]
-[[Category: Glycolytic enzyme]]
-[[Category: Lyase]]
-[[Category: Lyase-protein binding complex]]
-[[Category: Metal-binding]]
-[[Category: Protein-protein interaction]]

3h8a: Difference between revisions

Latest revision as of 07:17, 6 September 2023

Crystal structure of E. coli enolase bound to its cognate RNase E recognition domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

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