4u07: Difference between revisions
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''' | ==ATP bound to eukaryotic FIC domain containing protein== | ||
<StructureSection load='4u07' size='340' side='right' caption='[[4u07]], [[Resolution|resolution]] 2.64Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4u07]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U07 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U07 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uo4|4uo4]]</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=4u07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u07 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u07 RCSB], [http://www.ebi.ac.uk/pdbsum/4u07 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protein AMPylation, the transfer of AMP from ATP to protein targets, has been recognized as a new mechanism of host-cell disruption by some bacterial effectors that typically contain a FIC-domain. Eukaryotic genomes also encode one FIC-domain protein, HYPE, which has remained poorly characterized. Here we describe the structure of human HYPE, solved by X-ray crystallography, representing the first structure of a eukaryotic FIC-domain protein. We demonstrate that HYPE forms stable dimers with structurally and functionally integrated FIC-domains and with TPR-motifs exposed for protein-protein interactions. As HYPE also uniquely possesses a transmembrane helix, dimerization is likely to affect its positioning and function in the membrane vicinity. The low rate of autoAMPylation of the wild-type HYPE could be due to autoinhibition, consistent with the mechanism proposed for a number of putative FIC AMPylators. Our findings also provide a basis to further consider possible alternative cofactors of HYPE and distinct modes of target-recognition. | |||
Crystal Structure of the Human, FIC-Domain Containing Protein HYPE and Implications for Its Functions.,Bunney TD, Cole AR, Broncel M, Esposito D, Tate EW, Katan M Structure. 2014 Nov 25. pii: S0969-2126(14)00334-7. doi:, 10.1016/j.str.2014.10.007. PMID:25435325<ref>PMID:25435325</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bunney, T D]] | |||
[[Category: Cole, A R]] | |||
[[Category: Katan, M]] | |||
[[Category: Atp]] | |||
[[Category: Fic]] | |||
[[Category: Tpr]] | |||
[[Category: Transferase]] | |||
Revision as of 16:02, 10 December 2014
ATP bound to eukaryotic FIC domain containing protein
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