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| | ==Structure of DraG-GlnZ complex with ADP== | | ==Structure of DraG-GlnZ complex with ADP== |
| - | <StructureSection load='3o5t' size='340' side='right' caption='[[3o5t]], [[Resolution|resolution]] 2.09Å' scene=''> | + | <StructureSection load='3o5t' size='340' side='right'caption='[[3o5t]], [[Resolution|resolution]] 2.09Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3o5t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Azospirillum_brasilense Azospirillum brasilense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O5T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O5T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3o5t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Azospirillum_brasilense Azospirillum brasilense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O5T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</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]] 2.09Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">draG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=192 Azospirillum brasilense]), glnZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=192 Azospirillum brasilense])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ADP-ribosyl-[dinitrogen_reductase]_hydrolase ADP-ribosyl-[dinitrogen reductase] hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.24 3.2.2.24] </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=3o5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o5t OCA], [https://pdbe.org/3o5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o5t RCSB], [https://www.ebi.ac.uk/pdbsum/3o5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o5t 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=3o5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o5t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o5t RCSB], [http://www.ebi.ac.uk/pdbsum/3o5t PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A7XNI2_AZOBR A7XNI2_AZOBR] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3o5t" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Azospirillum brasilense]] | | [[Category: Azospirillum brasilense]] |
| - | [[Category: Li, X D]] | + | [[Category: Large Structures]] |
| - | [[Category: Rajendran, C]] | + | [[Category: Li X-D]] |
| - | [[Category: Winkler, F K]] | + | [[Category: Rajendran C]] |
| - | [[Category: Adp binding]] | + | [[Category: Winkler FK]] |
| - | [[Category: Hydrolase-transcription complex]]
| + | |
| Structural highlights
Function
A7XNI2_AZOBR
Publication Abstract from PubMed
Nitrogen metabolism in bacteria and archaea is regulated by a ubiquitous class of proteins belonging to the P(II)family. P(II) proteins act as sensors of cellular nitrogen, carbon, and energy levels, and they control the activities of a wide range of target proteins by protein-protein interaction. The sensing mechanism relies on conformational changes induced by the binding of small molecules to P(II) and also by P(II) posttranslational modifications. In the diazotrophic bacterium Azospirillum brasilense, high levels of extracellular ammonium inactivate the nitrogenase regulatory enzyme DraG by relocalizing it from the cytoplasm to the cell membrane. Membrane localization of DraG occurs through the formation of a ternary complex in which the P(II) protein GlnZ interacts simultaneously with DraG and the ammonia channel AmtB. Here we describe the crystal structure of the GlnZ-DraG complex at 2.1 A resolution, and confirm the physiological relevance of the structural data by site-directed mutagenesis. In contrast to other known P(II) complexes, the majority of contacts with the target protein do not involve the T-loop region of P(II). Hence this structure identifies a different mode of P(II) interaction with a target protein and demonstrates the potential for P(II) proteins to interact simultaneously with two different targets. A structural model of the AmtB-GlnZ-DraG ternary complex is presented. The results explain how the intracellular levels of ATP, ADP, and 2-oxoglutarate regulate the interaction between these three proteins and how DraG discriminates GlnZ from its close paralogue GlnB.
Crystal structure of the GlnZ-DraG complex reveals a different form of PII-target interaction.,Rajendran C, Gerhardt EC, Bjelic S, Gasperina A, Scarduelli M, Pedrosa FO, Chubatsu LS, Merrick M, Souza EM, Winkler FK, Huergo LF, Li XD Proc Natl Acad Sci U S A. 2011 Nov 22;108(47):18972-6. Epub 2011 Nov 9. PMID:22074780[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rajendran C, Gerhardt EC, Bjelic S, Gasperina A, Scarduelli M, Pedrosa FO, Chubatsu LS, Merrick M, Souza EM, Winkler FK, Huergo LF, Li XD. Crystal structure of the GlnZ-DraG complex reveals a different form of PII-target interaction. Proc Natl Acad Sci U S A. 2011 Nov 22;108(47):18972-6. Epub 2011 Nov 9. PMID:22074780 doi:http://dx.doi.org/10.1073/pnas.1108038108
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