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==Crystal Structure of the Ligand Binding Domain of E. coli IclR.==
==Crystal Structure of the Ligand Binding Domain of E. coli IclR.==
<StructureSection load='1td5' size='340' side='right' caption='[[1td5]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1td5' size='340' side='right'caption='[[1td5]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1td5]] is a 4 chain structure with 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=1TD5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TD5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1td5]] is a 4 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=1TD5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TD5 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1t9l|1t9l]], [[1tf1|1tf1]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ICLR, B4018 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=1td5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1td5 OCA], [https://pdbe.org/1td5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1td5 RCSB], [https://www.ebi.ac.uk/pdbsum/1td5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1td5 ProSAT], [https://www.topsan.org/Proteins/MCSG/1td5 TOPSAN]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1td5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1td5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1td5 RCSB], [http://www.ebi.ac.uk/pdbsum/1td5 PDBsum], [http://www.topsan.org/Proteins/MCSG/1td5 TOPSAN]</span></td></tr>
</table>
<table>
== Function ==
[https://www.uniprot.org/uniprot/ICLR_ECOLI ICLR_ECOLI] Regulation of the glyoxylate bypass operon (aceBAK), which encodes isocitrate lyase, malate synthase as well as isocitrate dehydrogenase kinase/phosphorylase. Glyoxylate disrupts the interaction with the promoter by favoring the inactive dimeric form. Pyruvate enhances promoter binding by stabilizing the tetrameric form.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/td/1td5_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/td/1td5_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=1td5 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
==See Also==
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Arrowsmith, C.]]
[[Category: Large Structures]]
[[Category: Bochkarev, A.]]
[[Category: Arrowsmith C]]
[[Category: Edwards, A.]]
[[Category: Bochkarev A]]
[[Category: Evdokimova, L.]]
[[Category: Edwards A]]
[[Category: Joachimiak, A.]]
[[Category: Evdokimova L]]
[[Category: MCSG, Midwest Center for Structural Genomics.]]
[[Category: Joachimiak A]]
[[Category: Savchenko, A.]]
[[Category: Savchenko A]]
[[Category: Walker, J R.]]
[[Category: Walker JR]]
[[Category: Zhang, R G.]]
[[Category: Zhang R-G]]
[[Category: Alpha/beta domain]]
[[Category: Ligand binding domain]]
[[Category: Mcsg]]
[[Category: Midwest center for structural genomic]]
[[Category: Protein structure initiative]]
[[Category: Psi]]
[[Category: Transcription]]
[[Category: Transcription regulator]]

Latest revision as of 10:27, 9 October 2024

Crystal Structure of the Ligand Binding Domain of E. coli IclR.Crystal Structure of the Ligand Binding Domain of E. coli IclR.

Structural highlights

1td5 is a 4 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 2.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

ICLR_ECOLI Regulation of the glyoxylate bypass operon (aceBAK), which encodes isocitrate lyase, malate synthase as well as isocitrate dehydrogenase kinase/phosphorylase. Glyoxylate disrupts the interaction with the promoter by favoring the inactive dimeric form. Pyruvate enhances promoter binding by stabilizing the tetrameric form.

Evolutionary Conservation

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

See Also

1td5, resolution 2.30Å

Drag the structure with the mouse to rotate

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OCA