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1ul3

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Revision as of 08:16, 28 March 2018

Crystal Structure of PII from Synechocystis sp. PCC 6803

Structural highlights

1ul3 is a 4 chain structure with sequence from Cyanobacterium synechocystis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	2pii, 1hwu
Gene:	GLNB (Cyanobacterium synechocystis)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GLNB_SYNY3] 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 (By similarity).

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 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 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^[1]

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

References

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ul3"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of PII from Synechocystis sp. PCC 6803==
 <StructureSection load='1ul3' size='340' side='right' caption='[[1ul3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pii|2pii]], [[1hwu|1hwu]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLNB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Cyanobacterium synechocystis])</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=1ul3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ul3 OCA], [http://pdbe.org/1ul3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ul3 RCSB], [http://www.ebi.ac.uk/pdbsum/1ul3 PDBsum]</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=1ul3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ul3 OCA], [http://pdbe.org/1ul3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ul3 RCSB], [http://www.ebi.ac.uk/pdbsum/1ul3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ul3 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ul/1ul3_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ul/1ul3_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1ul3

From Proteopedia

Revision as of 08:16, 28 March 2018

Crystal Structure of PII from Synechocystis sp. PCC 6803

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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