2eg2
From Proteopedia
(Difference between revisions)
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<StructureSection load='2eg2' size='340' side='right'caption='[[2eg2]], [[Resolution|resolution]] 1.72Å' scene=''> | <StructureSection load='2eg2' size='340' side='right'caption='[[2eg2]], [[Resolution|resolution]] 1.72Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2eg2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2eg2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EG2 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72Å</td></tr> |
| - | <tr id=' | + | <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=CL:CHLORIDE+ION'>CL</scene></td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2eg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eg2 OCA], [https://pdbe.org/2eg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eg2 RCSB], [https://www.ebi.ac.uk/pdbsum/2eg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eg2 ProSAT], [https://www.topsan.org/Proteins/RSGI/2eg2 TOPSAN]</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=2eg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eg2 OCA], [https://pdbe.org/2eg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eg2 RCSB], [https://www.ebi.ac.uk/pdbsum/2eg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eg2 ProSAT], [https://www.topsan.org/Proteins/RSGI/2eg2 TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/GLNB_AQUAE GLNB_AQUAE] In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS 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 (By similarity). | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Aquifex aeolicus | + | [[Category: Aquifex aeolicus]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Kitamura | + | [[Category: Kitamura Y]] |
| - | [[Category: Kuramitsu | + | [[Category: Kuramitsu S]] |
| - | + | [[Category: Sakai H]] | |
| - | [[Category: Sakai | + | [[Category: Shinkai A]] |
| - | [[Category: Shinkai | + | [[Category: Yokoyama S]] |
| - | [[Category: Yokoyama | + | |
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Current revision
The crystal structure of PII protein
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