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==Crystal structure of PhnF C-terminal domain==
==Crystal structure of PhnF C-terminal domain==
<StructureSection load='2fa1' size='340' side='right' caption='[[2fa1]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='2fa1' size='340' side='right'caption='[[2fa1]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2fa1]] is a 2 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=2FA1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FA1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2fa1]] is a 2 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=2FA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FA1 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BDF:BETA-D-FRUCTOPYRANOSE'>BDF</scene><br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">phnF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BDF:BETA-D-FRUCTOPYRANOSE'>BDF</scene></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=2fa1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fa1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fa1 RCSB], [http://www.ebi.ac.uk/pdbsum/2fa1 PDBsum], [http://www.topsan.org/Proteins/MCSG/2fa1 TOPSAN]</span></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=2fa1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fa1 OCA], [https://pdbe.org/2fa1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fa1 RCSB], [https://www.ebi.ac.uk/pdbsum/2fa1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fa1 ProSAT], [https://www.topsan.org/Proteins/MCSG/2fa1 TOPSAN]</span></td></tr>
<table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PHNF_ECOLI PHNF_ECOLI] Belongs to an operon involved in alkylphosphonate uptake and C-P lyase. Exact function not known. By similarity could be a transcriptional regulator.
== 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/fa/2fa1_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fa/2fa1_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2fa1 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of Escherichia coli PhnF C-terminal domain (C-PhnF) was solved at 1.7 A resolution by the single wavelength anomalous dispersion (SAD) method. The PhnF protein belongs to the HutC subfamily of the large GntR transcriptional regulator family. Members of this family share similar N-terminal DNA-binding domains, but are divided into four subfamilies according to their heterogenic C-terminal domains, which are involved in effector binding and oligomerization. The C-PhnF structure provides for the first time the scaffold of this domain for the HutC subfamily, which covers about 31% of GntR-like regulators. The structure represents a mixture of alpha-helices and beta-strands, with a six-stranded antiparallel beta-sheet at the core. C-PhnF monomers form a dimer by establishing interdomain eight-strand beta-sheets that include core antiparallel and N-terminal two-strand parallel beta-sheets from each monomer. C-PhnF shares strong structural similarity with the chorismate lyase fold, which features a buried active site locked behind two helix-turn-helix loops. The structural comparison of the C-PhnF and UbiC proteins allows us to propose that a similar site in the PhnF structure is adapted for effector binding.
Structural characterization of GntR/HutC family signaling domain.,Gorelik M, Lunin VV, Skarina T, Savchenko A Protein Sci. 2006 Jun;15(6):1506-11. Epub 2006 May 2. PMID:16672238<ref>PMID:16672238</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Edwards, A M.]]
[[Category: Large Structures]]
[[Category: Gorelik, M.]]
[[Category: Edwards AM]]
[[Category: Joachimiak, A.]]
[[Category: Gorelik M]]
[[Category: Lunin, V V.]]
[[Category: Joachimiak A]]
[[Category: MCSG, Midwest Center for Structural Genomics.]]
[[Category: Lunin VV]]
[[Category: Nocek, B P.]]
[[Category: Nocek BP]]
[[Category: Savchenko, A.]]
[[Category: Savchenko A]]
[[Category: Skarina, T.]]
[[Category: Skarina T]]
[[Category: Apc5558]]
[[Category: Effector binding domain]]
[[Category: Mcsg]]
[[Category: Midwest center for structural genomic]]
[[Category: Pnhf]]
[[Category: Protein structure initiative]]
[[Category: Psi]]
[[Category: Regulator]]
[[Category: Transcription]]

Latest revision as of 12:22, 14 February 2024

Crystal structure of PhnF C-terminal domainCrystal structure of PhnF C-terminal domain

Structural highlights

2fa1 is a 2 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 1.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

PHNF_ECOLI Belongs to an operon involved in alkylphosphonate uptake and C-P lyase. Exact function not known. By similarity could be a transcriptional regulator.

Evolutionary Conservation

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

2fa1, resolution 1.70Å

Drag the structure with the mouse to rotate

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OCA
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