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4u0z

From Proteopedia

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Eukaryotic Fic Domain containing protein with bound APCPP

Structural highlights

4u0z is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.95Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FICD_HUMAN Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins. Able to inactivate Rho GTPases in vitro by adding AMP to RhoA, Rac and Cdc42. It is however unclear whether it inactivates GTPases in vivo and physiological substrates probably remain to be identified.^[1] ^[2]

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Worby CA, Mattoo S, Kruger RP, Corbeil LB, Koller A, Mendez JC, Zekarias B, Lazar C, Dixon JE. The fic domain: regulation of cell signaling by adenylylation. Mol Cell. 2009 Apr 10;34(1):93-103. doi: 10.1016/j.molcel.2009.03.008. PMID:19362538 doi:http://dx.doi.org/10.1016/j.molcel.2009.03.008
↑ Engel P, Goepfert A, Stanger FV, Harms A, Schmidt A, Schirmer T, Dehio C. Adenylylation control by intra- or intermolecular active-site obstruction in Fic proteins. Nature. 2012 Jan 22;482(7383):107-10. doi: 10.1038/nature10729. PMID:22266942 doi:10.1038/nature10729
↑ Bunney TD, Cole AR, Broncel M, Esposito D, Tate EW, Katan M. Crystal Structure of the Human, FIC-Domain Containing Protein HYPE and Implications for Its Functions. Structure. 2014 Nov 25. pii: S0969-2126(14)00334-7. doi:, 10.1016/j.str.2014.10.007. PMID:25435325 doi:http://dx.doi.org/10.1016/j.str.2014.10.007

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4u0z"

Categories: Homo sapiens | Large Structures | Bunney TD | Cole AR | Katan M

@@ Line 1: / Line 1: @@
 ==Eukaryotic Fic Domain containing protein with bound APCPP==
-<StructureSection load='4u0z' size='340' side='right' caption='[[4u0z]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
+<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>
+<table><tr><td colspan='2'>[[4u0z]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uo4|4uo4]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4u0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u0z OCA], [https://pdbe.org/4u0z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u0z RCSB], [https://www.ebi.ac.uk/pdbsum/4u0z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u0z ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FICD_HUMAN FICD_HUMAN]] Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins. Able to inactivate Rho GTPases in vitro by adding AMP to RhoA, Rac and Cdc42. It is however unclear whether it inactivates GTPases in vivo and physiological substrates probably remain to be identified.<ref>PMID:19362538</ref> <ref>PMID:22266942</ref>
+[https://www.uniprot.org/uniprot/FICD_HUMAN FICD_HUMAN] Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins. Able to inactivate Rho GTPases in vitro by adding AMP to RhoA, Rac and Cdc42. It is however unclear whether it inactivates GTPases in vivo and physiological substrates probably remain to be identified.<ref>PMID:19362538</ref> <ref>PMID:22266942</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4u0z" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Fic protein 3D structures|Fic protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bunney, T D]]
+[[Category: Homo sapiens]]
-[[Category: Cole, A R]]
+[[Category: Large Structures]]
-[[Category: Katan, M]]
+[[Category: Bunney TD]]
-[[Category: Adenylation]]
+[[Category: Cole AR]]
-[[Category: Apcpp]]
+[[Category: Katan M]]
-[[Category: Fic]]
-[[Category: Tpr]]
-[[Category: Transferase]]

4u0z

From Proteopedia

Current revision

Eukaryotic Fic Domain containing protein with bound APCPP

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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