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3se5

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<StructureSection load='3se5' size='340' side='right'caption='[[3se5]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='3se5' size='340' side='right'caption='[[3se5]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3se5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Neimi Neimi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SE5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3se5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_B Neisseria meningitidis serogroup B]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SE5 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3s6a|3s6a]], [[2g03|2g03]], [[3sn9|3sn9]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NMB0255 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=491 NEIMI])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3se5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3se5 OCA], [https://pdbe.org/3se5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3se5 RCSB], [https://www.ebi.ac.uk/pdbsum/3se5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3se5 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=3se5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3se5 OCA], [https://pdbe.org/3se5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3se5 RCSB], [https://www.ebi.ac.uk/pdbsum/3se5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3se5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/NMFIC_NEIMB NMFIC_NEIMB]] Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins.
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[https://www.uniprot.org/uniprot/NMFIC_NEIMB NMFIC_NEIMB] Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Fic proteins that are defined by the ubiquitous FIC (filamentation induced by cyclic AMP) domain are known to catalyse adenylylation (also called AMPylation); that is, the transfer of AMP onto a target protein. In mammalian cells, adenylylation of small GTPases through Fic proteins injected by pathogenic bacteria can cause collapse of the actin cytoskeleton and cell death. It is unknown how this potentially deleterious adenylylation activity is regulated in the widespread Fic proteins that are found in all domains of life and that are thought to have critical roles in intrinsic signalling processes. Here we show that FIC-domain-mediated adenylylation is controlled by a conserved mechanism of ATP-binding-site obstruction that involves an inhibitory alpha-helix (alpha(inh)) with a conserved (S/T)XXXE(G/N) motif, and that in this mechanism the invariable glutamate competes with ATP gamma-phosphate binding. Consistent with this, FIC-domain-mediated growth arrest of bacteria by the VbhT toxin of Bartonella schoenbuchensis is intermolecularly repressed by the VbhA antitoxin through tight binding of its alpha(inh) to the FIC domain of VbhT, as shown by structure and function analysis. Furthermore, structural comparisons with other bacterial Fic proteins, such as Fic of Neisseria meningitidis and of Shewanella oneidensis, show that alpha(inh) frequently constitutes an amino-terminal or carboxy-terminal extension to the FIC domain, respectively, partially obstructing the ATP binding site in an intramolecular manner. After mutation of the inhibitory motif in various Fic proteins, including the human homologue FICD (also known as HYPE), adenylylation activity is considerably boosted, consistent with the anticipated relief of inhibition. Structural homology modelling of all annotated Fic proteins indicates that inhibition by alpha(inh) is universal and conserved through evolution, as the inhibitory motif is present in approximately 90% of all putatively adenylylation-active FIC domains, including examples from all domains of life and from viruses. Future studies should reveal how intrinsic or extrinsic factors modulate adenylylation activity by weakening the interaction of alpha(inh) with the FIC active site.
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Adenylylation control by intra- or intermolecular active-site obstruction in Fic proteins.,Engel P, Goepfert A, Stanger FV, Harms A, Schmidt A, Schirmer T, Dehio C Nature. 2012 Jan 22;482(7383):107-10. doi: 10.1038/nature10729. PMID:22266942<ref>PMID:22266942</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3se5" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Fic protein 3D structures|Fic protein 3D structures]]
*[[Fic protein 3D structures|Fic protein 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Neimi]]
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[[Category: Neisseria meningitidis serogroup B]]
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[[Category: Goepfert, A]]
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[[Category: Goepfert A]]
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[[Category: Schirmer, T]]
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[[Category: Schirmer T]]
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[[Category: Stanger, F]]
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[[Category: Stanger F]]
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[[Category: Adenylylation]]
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[[Category: Ampylation]]
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[[Category: Transferase]]
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Current revision

Fic protein from NEISSERIA MENINGITIDIS mutant delta8 in complex with AMPPNP

PDB ID 3se5

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