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2rd5

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{{Seed}}
 
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[[Image:2rd5.png|left|200px]]
 
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==Structural basis for the regulation of N-acetylglutamate kinase by PII in Arabidopsis thaliana==
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The line below this paragraph, containing "STRUCTURE_2rd5", creates the "Structure Box" on the page.
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<StructureSection load='2rd5' size='340' side='right'caption='[[2rd5]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2rd5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RD5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RD5 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.51&#8491;</td></tr>
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<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=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NLG:N-ACETYL-L-GLUTAMATE'>NLG</scene></td></tr>
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{{STRUCTURE_2rd5| PDB=2rd5 | SCENE= }}
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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=2rd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rd5 OCA], [https://pdbe.org/2rd5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rd5 RCSB], [https://www.ebi.ac.uk/pdbsum/2rd5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rd5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NAGK_ARATH NAGK_ARATH] Involved in the arginine biosynthetic pathway via the intermediate compound ornithine.<ref>PMID:16377628</ref> <ref>PMID:16545809</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rd/2rd5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2rd5 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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PII is a highly conserved regulatory protein found in organisms across the three domains of life. In cyanobacteria and plants, PII relieves the feedback inhibition of the rate-limiting step in arginine biosynthesis catalyzed by N-acetylglutamate kinase (NAGK). To understand the molecular structural basis of enzyme regulation by PII, we have determined a 2.5-A resolution crystal structure of a complex formed between two homotrimers of PII and a single hexamer of NAGK from Arabidopsis thaliana bound to the metabolites N-acetylglutamate, ADP, ATP, and arginine. In PII, the T-loop and Trp(22) at the start of the alpha1-helix, which are both adjacent to the ATP-binding site of PII, contact two beta-strands as well as the ends of two central helices (alphaE and alphaG) in NAGK, the opposing ends of which form major portions of the ATP and N-acetylglutamate substrate-binding sites. The binding of Mg(2+).ATP to PII stabilizes a conformation of the T-loop that favors interactions with both open and closed conformations of NAGK. Interactions between PII and NAGK appear to limit the degree of opening and closing of the active-site cleft in opposition to a domain-separating inhibitory effect exerted by arginine, thus explaining the stimulatory effect of PII on the kinetics of arginine-inhibited NAGK.
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===Structural basis for the regulation of N-acetylglutamate kinase by PII in Arabidopsis thaliana===
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Structural basis for the regulation of N-acetylglutamate kinase by PII in Arabidopsis thaliana.,Mizuno Y, Moorhead GB, Ng KK J Biol Chem. 2007 Dec 7;282(49):35733-40. Epub 2007 Oct 3. PMID:17913711<ref>PMID:17913711</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_17913711}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2rd5" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17913711 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17913711}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2RD5 is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RD5 OCA].
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==Reference==
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<ref group="xtra">PMID:17913711</ref><references group="xtra"/>
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[[Category: Acetylglutamate kinase]]
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[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: Mizuno, Y.]]
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[[Category: Large Structures]]
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[[Category: Moorhead, G B.G.]]
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[[Category: Mizuno Y]]
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[[Category: Ng, K K.S.]]
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[[Category: Moorhead GBG]]
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[[Category: Kinase]]
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[[Category: Ng KKS]]
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[[Category: Nitrogen metabolism]]
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[[Category: Protein binding]]
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[[Category: Protein-protein complex]]
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[[Category: Regulation of arginine biosynthesis]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 04:59:10 2009''
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Current revision

Structural basis for the regulation of N-acetylglutamate kinase by PII in Arabidopsis thaliana

PDB ID 2rd5

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