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| | <StructureSection load='5jff' size='340' side='right'caption='[[5jff]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='5jff' size='340' side='right'caption='[[5jff]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jff]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JFF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5JFF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jff]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JFF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JFF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=144:TRIS-HYDROXYMETHYL-METHYL-AMMONIUM'>144</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fic, b3361, JW3324 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), yhfG, b3362, JW3325 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=144:TRIS-HYDROXYMETHYL-METHYL-AMMONIUM'>144</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5jff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jff OCA], [http://pdbe.org/5jff PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jff RCSB], [http://www.ebi.ac.uk/pdbsum/5jff PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jff ProSAT]</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=5jff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jff OCA], [https://pdbe.org/5jff PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jff RCSB], [https://www.ebi.ac.uk/pdbsum/5jff PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jff ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FIC_ECOLI FIC_ECOLI]] Probable adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (By similarity). Involved in cell filamentation induced by cyclic AMP. May have some role in cell division. | + | [https://www.uniprot.org/uniprot/FIC_ECOLI FIC_ECOLI] Probable adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (By similarity). Involved in cell filamentation induced by cyclic AMP. May have some role in cell division. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Schirmer, T]] | + | [[Category: Schirmer T]] |
| - | [[Category: Stanger, F V]] | + | [[Category: Stanger FV]] |
| - | [[Category: Class i fic protein]]
| + | |
| - | [[Category: Fic domain]]
| + | |
| - | [[Category: Fic-1]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
FIC_ECOLI Probable adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (By similarity). Involved in cell filamentation induced by cyclic AMP. May have some role in cell division.
Publication Abstract from PubMed
FIC domain proteins mediate post-translational modifications of target proteins, which typically results in their inactivation. Depending on the conservation of crucial active site residues, the FIC fold serves as structural scaffold for various enzymatic activities, mostly target adenylylation. The founding member of the vast Fic protein family, EcFicT, was identified in Escherichia coli some time ago. The G55R point mutant of EcFicT displays the "filamentation induced by cAMP" (Fic) phenotype at high 3',5'-cyclic adenosine monophosphate (cAMP) concentrations and elevated temperature, but the underlying molecular mechanism and any putative biochemical activity of EcFicT have remained unknown. EcFicT belongs to class I Fic toxin proteins that are encoded together with a small inhibitory protein (antitoxin), named EcFicA in E. coli. Here, we report the crystal structures of two mutant EcFicT/EcFicA complexes (EcFicTG55RA and EcFicTAE28G) both showing close resemblance with the structure of the AMP-transferase VbhT from Bartonella schoenbuchensis in complex with its cognate antitoxin VbhA. However, crucial differences in the active site of EcFicT compared to VbhT and other AMP-transferases rationalize the lack of evidence for adenylylation activity. Comprehensive bioinformatic analysis suggests that EcFicT has evolved from canonical AMP-transferases and has acquired a conserved binding site for a yet to be discovered novel substrate. The G55R mutation has no effect on structure or thermal stability of EcFicT, such that the molecular basis for its associated Fic phenotype remains elusive. We anticipate that this structure will inspire further bioinformatic and experimental analyses in order to characterize the enzymatic activity of EcFicT and help revealing its physiological role.
Crystal Structure of the Escherichia coli Fic Toxin-Like Protein in Complex with Its Cognate Antitoxin.,Stanger FV, Harms A, Dehio C, Schirmer T PLoS One. 2016 Sep 22;11(9):e0163654. doi: 10.1371/journal.pone.0163654., eCollection 2016. PMID:27657533[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Stanger FV, Harms A, Dehio C, Schirmer T. Crystal Structure of the Escherichia coli Fic Toxin-Like Protein in Complex with Its Cognate Antitoxin. PLoS One. 2016 Sep 22;11(9):e0163654. doi: 10.1371/journal.pone.0163654., eCollection 2016. PMID:27657533 doi:http://dx.doi.org/10.1371/journal.pone.0163654
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