2eg2
From Proteopedia
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==The crystal structure of PII protein== | ==The crystal structure of PII protein== | ||
- | <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 [ | + | <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> |
- | < | + | <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'>[ | + | |
</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]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
- | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eg/2eg2_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eg/2eg2_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Aquifex aeolicus | + | [[Category: Aquifex aeolicus]] |
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Kitamura Y]] |
- | [[Category: | + | [[Category: Kuramitsu S]] |
- | [[Category: Sakai | + | [[Category: Sakai H]] |
- | [[Category: Shinkai | + | [[Category: Shinkai A]] |
- | [[Category: Yokoyama | + | [[Category: Yokoyama S]] |
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Current revision
The crystal structure of PII protein
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