2fa1

<StructureSection load='2fa1' size='340' side='right' caption='[[2fa1]], [[Resolution|resolution]] 1.70&Aring;' scene=''>

<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>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BDF:BETA-D-FRUCTOPYRANOSE'>BDF</scene></td></tr>

<tr id='gene'><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='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=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>

[[http://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.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fa/2fa1_consurf.spt"</scriptWhenChecked>

</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].

<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>

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== References ==

<references/>

[[Category: Edwards, A M]]

[[Category: Gorelik, M]]

[[Category: Joachimiak, A]]

[[Category: Lunin, V V]]

[[Category: Structural genomic]]

[[Category: Nocek, B P]]

[[Category: Savchenko, A]]

[[Category: Skarina, T]]

[[Category: Transcription]]