8cil

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'''Unreleased structure'''
 
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The entry 8cil is ON HOLD until Paper Publication
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==Crystal structure of Coxiella burnetii Fic protein 2==
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<StructureSection load='8cil' size='340' side='right'caption='[[8cil]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8cil]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Coxiella_burnetii Coxiella burnetii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CIL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CIL FirstGlance]. <br>
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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]] 1.98&#8491;</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=8cil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cil OCA], [https://pdbe.org/8cil PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cil RCSB], [https://www.ebi.ac.uk/pdbsum/8cil PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cil ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q83DB6_COXBU Q83DB6_COXBU]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The intracellular bacterial pathogen Coxiella burnetii evades the host response by secreting effector proteins that aid in establishing a replication-friendly niche. Bacterial filamentation induced by cyclic AMP (Fic) enzymes can act as effectors by covalently modifying target proteins with the posttranslational AMPylation by transferring adenosine monophosphate (AMP) from adenosine triphosphate (ATP) to a hydroxyl-containing side chain. Here we identify the gene product of C. burnetii CBU_0822, termed C. burnetii Fic 2 (CbFic2), to AMPylate host cell histone H3 at serine 10 and serine 28. We show that CbFic2 acts as a bifunctional enzyme, both capable of AMPylation as well as deAMPylation, and is regulated by the binding of DNA via a C-terminal helix-turn-helix domain. We propose that CbFic2 performs AMPylation in its monomeric state, switching to a deAMPylating dimer upon DNA binding. This study unveils reversible histone modification by a specific enzyme of a pathogenic bacterium.
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Authors: Hoepfner, D., Itzen, A., Pogenberg, V.
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The DNA-binding induced (de)AMPylation activity of a Coxiella burnetii Fic enzyme targets Histone H3.,Hopfner D, Cichy A, Pogenberg V, Krisp C, Mezouar S, Bach NC, Grotheer J, Zarza SM, Martinez E, Bonazzi M, Feige MJ, Sieber SA, Schluter H, Itzen A Commun Biol. 2023 Nov 6;6(1):1124. doi: 10.1038/s42003-023-05494-7. PMID:37932372<ref>PMID:37932372</ref>
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Description: Crystal structure of Coxiella burnetii Fic protein 2
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Itzen, A]]
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<div class="pdbe-citations 8cil" style="background-color:#fffaf0;"></div>
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[[Category: Pogenberg, V]]
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== References ==
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[[Category: Hoepfner, D]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Coxiella burnetii]]
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[[Category: Large Structures]]
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[[Category: Hoepfner D]]
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[[Category: Itzen A]]
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[[Category: Pogenberg V]]

Revision as of 07:31, 15 November 2023

Crystal structure of Coxiella burnetii Fic protein 2

PDB ID 8cil

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