2pii: Difference between revisions

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New page: left|200px<br /><applet load="2pii" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pii, resolution 1.9Å" /> '''PII, GLNB PRODUCT'''<...
 
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[[Image:2pii.jpg|left|200px]]<br /><applet load="2pii" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2pii, resolution 1.9&Aring;" />
'''PII, GLNB PRODUCT'''<br />


==Overview==
==PII, GLNB PRODUCT==
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.
<StructureSection load='2pii' size='340' side='right'caption='[[2pii]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<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>
2PII is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2PII OCA].  
</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>
 
<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>
==Reference==
</table>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299730 15299730]
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pi/2pii_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=2pii ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Carr, P.D.]]
[[Category: Carr PD]]
[[Category: Cheah, E.]]
[[Category: Cheah E]]
[[Category: Ollis, D.L.]]
[[Category: Ollis DL]]
[[Category: Suffolk, P.M.]]
[[Category: Suffolk PM]]
[[Category: signal transduction protein]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:33:11 2007''

Latest revision as of 12:09, 21 February 2024

PII, GLNB PRODUCTPII, GLNB PRODUCT

Structural highlights

2pii is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Evolutionary Conservation

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

2pii, resolution 1.90Å

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OCA
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