4u0z: Difference between revisions

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'''Unreleased structure'''
==Eukaryotic Fic Domain containing protein with bound APCPP==
<StructureSection load='4u0z' size='340' side='right' caption='[[4u0z]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4u0z]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U0Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U0Z FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4u0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u0z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u0z RCSB], [http://www.ebi.ac.uk/pdbsum/4u0z 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.


The entry 4u0z is ON HOLD
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>


Authors: Cole, A.R., Bunney, T.D., Katan, M.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description:
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bunney, T D]]
[[Category: Cole, A R]]
[[Category: Katan, M]]
[[Category: Adenylation]]
[[Category: Apcpp]]
[[Category: Fic]]
[[Category: Tpr]]
[[Category: Transferase]]
Retrieved from "https://proteopedia.org/4u0z"