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| | <StructureSection load='5cgl' size='340' side='right'caption='[[5cgl]], [[Resolution|resolution]] 2.35Å' scene=''> | | <StructureSection load='5cgl' size='340' side='right'caption='[[5cgl]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5cgl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"diplokokkus_intracellularis_meningitidis"_(sic)_weichselbaum_1887 "diplokokkus intracellularis meningitidis" (sic) weichselbaum 1887]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CGL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CGL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5cgl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CGL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NMB0255 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=487 "Diplokokkus intracellularis meningitidis" (sic) Weichselbaum 1887])</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=5cgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cgl OCA], [https://pdbe.org/5cgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cgl RCSB], [https://www.ebi.ac.uk/pdbsum/5cgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cgl ProSAT]</span></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=5cgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cgl OCA], [http://pdbe.org/5cgl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cgl RCSB], [http://www.ebi.ac.uk/pdbsum/5cgl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cgl ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NMFIC_NEIMB NMFIC_NEIMB]] Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins. | + | [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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Schirmer, T]] | + | [[Category: Neisseria meningitidis]] |
| - | [[Category: Stanger, F V]] | + | [[Category: Schirmer T]] |
| - | [[Category: Amp-transferase]] | + | [[Category: Stanger FV]] |
| - | [[Category: Dimer]]
| + | |
| - | [[Category: Fic protein]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
NMFIC_NEIMB Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins.
Publication Abstract from PubMed
Filamentation induced by cyclic AMP (FIC)-domain enzymes catalyze adenylylation or other posttranslational modifications of target proteins to control their function. Recently, we have shown that Fic enzymes are autoinhibited by an alpha-helix (alphainh) that partly obstructs the active site. For the single-domain class III Fic proteins, the alphainh is located at the C terminus and its deletion relieves autoinhibition. However, it has remained unclear how activation occurs naturally. Here, we show by structural, biophysical, and enzymatic analyses combined with in vivo data that the class III Fic protein NmFic from Neisseria meningitidis gets autoadenylylated in cis, thereby autonomously relieving autoinhibition and thus allowing subsequent adenylylation of its target, the DNA gyrase subunit GyrB. Furthermore, we show that NmFic activation is antagonized by tetramerization. The combination of autoadenylylation and tetramerization results in nonmonotonic concentration dependence of NmFic activity and a pronounced lag phase in the progress of target adenylylation. Bioinformatic analyses indicate that this elaborate dual-control mechanism is conserved throughout class III Fic proteins.
Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification.,Stanger FV, Burmann BM, Harms A, Aragao H, Mazur A, Sharpe T, Dehio C, Hiller S, Schirmer T Proc Natl Acad Sci U S A. 2016 Jan 19. pii: 201516930. PMID:26787847[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Stanger FV, Burmann BM, Harms A, Aragao H, Mazur A, Sharpe T, Dehio C, Hiller S, Schirmer T. Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification. Proc Natl Acad Sci U S A. 2016 Jan 19. pii: 201516930. PMID:26787847 doi:http://dx.doi.org/10.1073/pnas.1516930113
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