1qy7: Difference between revisions

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[[Image:1qy7.png|left|200px]]


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==The structure of the PII protein from the cyanobacteria Synechococcus sp. PCC 7942==
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<StructureSection load='1qy7' size='340' side='right'caption='[[1qy7]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qy7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_7942_=_FACHB-805 Synechococcus elongatus PCC 7942 = FACHB-805]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QY7 FirstGlance]. <br>
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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&#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=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_1qy7|  PDB=1qy7  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qy7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qy7 OCA], [https://pdbe.org/1qy7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qy7 RCSB], [https://www.ebi.ac.uk/pdbsum/1qy7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qy7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLNB_SYNE7 GLNB_SYNE7] 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 phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qy/1qy7_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=1qy7 ConSurf].
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== Publication Abstract from PubMed ==
The PII proteins from the cyanobacteria Synechococcus sp. PCC 7942 and Synechocystis sp. PCC 6803 have been crystallized and high-resolution structures have been obtained using X-ray crystallography. The core of these new structures is similar to that of the PII proteins from Escherichia coli, although the structures of the T- and C-loops differ. The T-loop of the Synechococcus protein is ordered, but appears to be stabilized by crystal contacts. The same loop in the Synechocystis protein is disordered. The C-terminus of the Synechocystis protein is stabilized by hydrogen bonding to the same region of a crystallographically related molecule. The same terminus in the Synechococcus protein is stabilized by coordination with a metal ion. These observations are consistent with the idea that both the T-loop and the C-terminus of PII proteins are flexible in solution and that this flexibility may be important for receptor recognition. Sequence comparisons are used to identify regions of the sequence unique to the cyanobacteria.


===The structure of the PII protein from the cyanobacteria Synechococcus sp. PCC 7942===
The structures of the PII proteins from the cyanobacteria Synechococcus sp. PCC 7942 and Synechocystis sp. PCC 6803.,Xu Y, Carr PD, Clancy P, Garcia-Dominguez M, Forchhammer K, Florencio F, Vasudevan SG, Tandeau de Marsac N, Ollis DL Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2183-90. Epub 2003, Nov 27. PMID:14646076<ref>PMID:14646076</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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(as it appears on PubMed at http://www.pubmed.gov), where 14646076 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_14646076}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1QY7 is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Synechococcus_sp. Synechococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QY7 OCA].
[[Category: Synechococcus elongatus PCC 7942 = FACHB-805]]
 
[[Category: Carr PD]]
==Reference==
[[Category: Clancy P]]
<ref group="xtra">PMID:14646076</ref><references group="xtra"/>
[[Category: Florencio F]]
[[Category: Synechococcus sp.]]
[[Category: Forchhammer K]]
[[Category: Carr, P D.]]
[[Category: Garcia-Dominguez M]]
[[Category: Clancy, P.]]
[[Category: Ollis DL]]
[[Category: Florencio, F.]]
[[Category: Tandeau de Marsac N]]
[[Category: Forchhammer, K.]]
[[Category: Vasudevan SG]]
[[Category: Garcia-Dominguez, M.]]
[[Category: Xu Y]]
[[Category: Marsac, N Tandeau de.]]
[[Category: Ollis, D L.]]
[[Category: Vasudevan, S G.]]
[[Category: Xu, Y.]]
[[Category: Alpha/beta]]
 
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