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2pii

From Proteopedia

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[[Image:2pii.jpg|left|200px]]
 
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{{Structure
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==PII, GLNB PRODUCT==
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|PDB= 2pii |SIZE=350|CAPTION= <scene name='initialview01'>2pii</scene>, resolution 1.9&Aring;
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<StructureSection load='2pii' size='340' side='right'caption='[[2pii]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[2pii]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PII FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.9&#8491;</td></tr>
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|GENE= GLNB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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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=2pii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pii OCA], [https://pdbe.org/2pii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pii RCSB], [https://www.ebi.ac.uk/pdbsum/2pii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pii ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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'''PII, GLNB PRODUCT'''
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[https://www.uniprot.org/uniprot/GLNB_ECOLI GLNB_ECOLI] P-II indirectly controls the transcription of the glutamine synthetase 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 uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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The structure of the bacterial signal transduction protein P(II) has been refined to an R factor of 13.2% using 3sigma data between 10 and 1.9 A. The crystals exhibited twinning by merohedry and X-ray intensities were corrected using the method of Fisher &amp; Sweet [Fisher &amp; Sweet (1980). Acta Cryst. A36, 755-760] prior to refinement. Our earlier 2.7 A structure [Cheah, Carr, Suffolk, Vasudevan, Dixon &amp; Ollis (1994). Structure, 2, 981-990] served as a starting model. P(II) is a trimeric molecule, each subunit has a mass of 12.4 kDa and contains 112 amino-acid residues. The refined model includes all 1065 protein atoms per subunit plus 312 water molecules. The high-resolution refinement confirms the correctness of our 2.7 A model, although it leads to a redefinition of the extent of various secondary-structural elements. The monomeric structure of P(II) exhibits an interlocking double betaalphabeta fold. This is a stable fold found in a number of proteins with diverse functions. The association of the protein into a trimer leads to a new structure which we describe in detail. The effects of crystal packing forces are discussed and potential interaction sites with other proteins and effector molecules are identified.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pi/2pii_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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2PII is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PII OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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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=2pii ConSurf].
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X-ray structure of the signal transduction protein from Escherichia coli at 1.9 A., Carr PD, Cheah E, Suffolk PM, Vasudevan SG, Dixon NE, Ollis DL, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):93-104. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299730 15299730]
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Carr, P D.]]
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[[Category: Carr PD]]
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[[Category: Cheah, E.]]
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[[Category: Cheah E]]
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[[Category: Ollis, D L.]]
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[[Category: Ollis DL]]
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[[Category: Suffolk, P M.]]
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[[Category: Suffolk PM]]
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[[Category: signal transduction protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:13:22 2008''
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Current revision

PII, GLNB PRODUCT

PDB ID 2pii

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