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| | ==Structure of uridylylated GlnB from Escherichia coli bound to ATP== | | ==Structure of uridylylated GlnB from Escherichia coli bound to ATP== |
| - | <StructureSection load='5l9n' size='340' side='right' caption='[[5l9n]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='5l9n' size='340' side='right'caption='[[5l9n]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5l9n]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L9N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L9N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5l9n]] is a 1 chain structure with sequence from [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=5L9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L9N FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <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]] 1.901Å</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=5l9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l9n OCA], [http://pdbe.org/5l9n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l9n RCSB], [http://www.ebi.ac.uk/pdbsum/5l9n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l9n ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=5l9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l9n OCA], [https://pdbe.org/5l9n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l9n RCSB], [https://www.ebi.ac.uk/pdbsum/5l9n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l9n ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GLNB_ECOLI GLNB_ECOLI]] P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme. | + | [https://www.uniprot.org/uniprot/GLNB_ECOLI GLNB_ECOLI] P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme. |
| | <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: Palanca, C]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Rubio, V]] | + | [[Category: Large Structures]] |
| - | [[Category: Glnk]] | + | [[Category: Palanca C]] |
| - | [[Category: Nitrogen metabolism]] | + | [[Category: Rubio V]] |
| - | [[Category: Pii protein]]
| + | |
| - | [[Category: Signaling protein]]
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| - | [[Category: Uridylylation]]
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| Structural highlights
Function
GLNB_ECOLI P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme.
Publication Abstract from PubMed
To adapt to environments with variable nitrogen sources and richness, the widely distributed homotrimeric PII signaling proteins bind their allosteric effectors ADP/ATP/2-oxoglutarate, and experience nitrogen-sensitive uridylylation of their flexible T-loops at Tyr51, regulating their interactions with effector proteins. To clarify whether uridylylation triggers a given T-loop conformation, we determined the crystal structure of the classical paradigm of PII protein, Escherichia coli GlnB (EcGlnB), in fully uridylylated form (EcGlnB-UMP3 ). This is the first structure of a postranslationally modified PII protein. This required recombinant production and purification of the uridylylating enzyme GlnD and its use for full uridylylation of large amounts of recombinantly produced pure EcGlnB. Unlike crystalline non-uridylylated EcGlnB, in which T-loops are fixed, uridylylation rendered the T-loop highly mobile because of loss of contacts mediated by Tyr51, with concomitant abolition of T-loop anchoring via Arg38 on the ATP site. This site was occupied by ATP, providing the first, long-sought snapshot of the EcGlnB-ATP complex, connecting ATP binding with T-loop changes. Inferences are made on the mechanisms of PII selectivity for ATP and of PII-UMP3 signaling, proposing a model for the architecture of the complex of EcGlnB-UMP3 with the uridylylation-sensitive PII target ATase (which adenylylates/deadenylylates glutamine synthetase) and with glutamine synthetase. This article is protected by copyright. All rights reserved.
Effects of T-loop modification on the PII-signaling protein: Structure of uridylylated Escherichia coli GlnB bound to ATP.,Palanca C, Rubio V Environ Microbiol Rep. 2017 Mar 26. doi: 10.1111/1758-2229.12533. PMID:28345298[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Palanca C, Rubio V. Effects of T-loop modification on the PII-signaling protein: Structure of uridylylated Escherichia coli GlnB bound to ATP. Environ Microbiol Rep. 2017 Mar 26. doi: 10.1111/1758-2229.12533. PMID:28345298 doi:http://dx.doi.org/10.1111/1758-2229.12533
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