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[[Image:2o67.jpg|left|200px]]


{{Structure
==Crystal structure of Arabidopsis thaliana PII bound to malonate==
|PDB= 2o67 |SIZE=350|CAPTION= <scene name='initialview01'>2o67</scene>, resolution 2.50&Aring;
<StructureSection load='2o67' size='340' side='right'caption='[[2o67]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>
<table><tr><td colspan='2'>[[2o67]] is a 3 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=2O67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O67 FirstGlance]. <br>
|ACTIVITY=
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
|GENE= AT4g01900, T7B11.16 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o67 OCA], [https://pdbe.org/2o67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o67 RCSB], [https://www.ebi.ac.uk/pdbsum/2o67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o67 ProSAT]</span></td></tr>
|RELATEDENTRY=[[2o66|2O66]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o67 OCA], [http://www.ebi.ac.uk/pdbsum/2o67 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2o67 RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/GLNB_ARATH GLNB_ARATH] Participates in sensing carbon and organic nitrogen status and regulates some steps of primary carbon and nitrogen metabolism. Required for nitrite uptake in chloroplasts and regulates arginine biosynthesis through interaction with acetylglutamate kinase (NAGK) in chloroplasts. Regulates fatty acids synthesis in chloroplasts by interacting with the acetyl-CoA carboxylase complex and inhibiting acetyl-CoA carboxylase (ACCase) activity.<ref>PMID:16133214</ref> <ref>PMID:18325336</ref> <ref>PMID:9811909</ref>
 
== Evolutionary Conservation ==
'''Crystal structure of Arabidopsis thaliana PII bound to malonate'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o6/2o67_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2o67 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 1.9 A resolution crystal structure of PII from Arabidopsis thaliana reveals for the first time the molecular structure of a widely conserved regulator of carbon and nitrogen metabolism from a eukaryote. The structure provides a framework for understanding the arrangement of highly conserved residues shared with PII proteins from bacteria, archaea, and red algae as well as residues conserved only in plant PII. Most strikingly, a highly conserved segment at the N-terminus that is found only in plant PII forms numerous interactions with the alpha2 helix and projects from the surface of the homotrimer opposite to that occupied by the T-loop. In addition, solvent-exposed residues near the T-loop are highly conserved in plants but differ in prokaryotes. Several residues at the C-terminus that are also highly conserved only in plants contribute part of the ATP-binding site and likely participate in an ATP-induced conformational change. Structures of PII also reveal how citrate and malonate bind near the triphosphate binding site occupied by ATP in bacterial and archaeal PII proteins.
The 1.9 A resolution crystal structure of PII from Arabidopsis thaliana reveals for the first time the molecular structure of a widely conserved regulator of carbon and nitrogen metabolism from a eukaryote. The structure provides a framework for understanding the arrangement of highly conserved residues shared with PII proteins from bacteria, archaea, and red algae as well as residues conserved only in plant PII. Most strikingly, a highly conserved segment at the N-terminus that is found only in plant PII forms numerous interactions with the alpha2 helix and projects from the surface of the homotrimer opposite to that occupied by the T-loop. In addition, solvent-exposed residues near the T-loop are highly conserved in plants but differ in prokaryotes. Several residues at the C-terminus that are also highly conserved only in plants contribute part of the ATP-binding site and likely participate in an ATP-induced conformational change. Structures of PII also reveal how citrate and malonate bind near the triphosphate binding site occupied by ATP in bacterial and archaeal PII proteins.


==About this Structure==
Crystal structure of Arabidopsis PII reveals novel structural elements unique to plants.,Mizuno Y, Berenger B, Moorhead GB, Ng KK Biochemistry. 2007 Feb 13;46(6):1477-83. PMID:17279613<ref>PMID:17279613</ref>
2O67 is a [[Single protein]] structure of sequence 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=2O67 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of Arabidopsis PII reveals novel structural elements unique to plants., Mizuno Y, Berenger B, Moorhead GB, Ng KK, Biochemistry. 2007 Feb 13;46(6):1477-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17279613 17279613]
</div>
<div class="pdbe-citations 2o67" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Berenger, B.]]
[[Category: Berenger B]]
[[Category: Mizuno, Y M.]]
[[Category: Mizuno YM]]
[[Category: Moorhead, G B.G.]]
[[Category: Moorhead GBG]]
[[Category: Ng, K K.S.]]
[[Category: Ng KKS]]
[[Category: regulation of nitrogen and carbon metabolism]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:13:18 2008''

Latest revision as of 13:31, 30 August 2023

Crystal structure of Arabidopsis thaliana PII bound to malonateCrystal structure of Arabidopsis thaliana PII bound to malonate

Structural highlights

2o67 is a 3 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GLNB_ARATH Participates in sensing carbon and organic nitrogen status and regulates some steps of primary carbon and nitrogen metabolism. Required for nitrite uptake in chloroplasts and regulates arginine biosynthesis through interaction with acetylglutamate kinase (NAGK) in chloroplasts. Regulates fatty acids synthesis in chloroplasts by interacting with the acetyl-CoA carboxylase complex and inhibiting acetyl-CoA carboxylase (ACCase) activity.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The 1.9 A resolution crystal structure of PII from Arabidopsis thaliana reveals for the first time the molecular structure of a widely conserved regulator of carbon and nitrogen metabolism from a eukaryote. The structure provides a framework for understanding the arrangement of highly conserved residues shared with PII proteins from bacteria, archaea, and red algae as well as residues conserved only in plant PII. Most strikingly, a highly conserved segment at the N-terminus that is found only in plant PII forms numerous interactions with the alpha2 helix and projects from the surface of the homotrimer opposite to that occupied by the T-loop. In addition, solvent-exposed residues near the T-loop are highly conserved in plants but differ in prokaryotes. Several residues at the C-terminus that are also highly conserved only in plants contribute part of the ATP-binding site and likely participate in an ATP-induced conformational change. Structures of PII also reveal how citrate and malonate bind near the triphosphate binding site occupied by ATP in bacterial and archaeal PII proteins.

Crystal structure of Arabidopsis PII reveals novel structural elements unique to plants.,Mizuno Y, Berenger B, Moorhead GB, Ng KK Biochemistry. 2007 Feb 13;46(6):1477-83. PMID:17279613[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Ferrario-Mery S, Bouvet M, Leleu O, Savino G, Hodges M, Meyer C. Physiological characterisation of Arabidopsis mutants affected in the expression of the putative regulatory protein PII. Planta. 2005 Dec;223(1):28-39. Epub 2005 Aug 16. PMID:16133214 doi:http://dx.doi.org/10.1007/s00425-005-0063-5
  2. ↑ Ferrario-Mery S, Meyer C, Hodges M. Chloroplast nitrite uptake is enhanced in Arabidopsis PII mutants. FEBS Lett. 2008 Apr 2;582(7):1061-6. doi: 10.1016/j.febslet.2008.02.056. Epub, 2008 Mar 4. PMID:18325336 doi:http://dx.doi.org/10.1016/j.febslet.2008.02.056
  3. ↑ Hsieh MH, Lam HM, van de Loo FJ, Coruzzi G. A PII-like protein in Arabidopsis: putative role in nitrogen sensing. Proc Natl Acad Sci U S A. 1998 Nov 10;95(23):13965-70. PMID:9811909
  4. ↑ Mizuno Y, Berenger B, Moorhead GB, Ng KK. Crystal structure of Arabidopsis PII reveals novel structural elements unique to plants. Biochemistry. 2007 Feb 13;46(6):1477-83. PMID:17279613 doi:10.1021/bi062149e

2o67, resolution 2.50Å

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