6w3j: Difference between revisions
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==Crystal structure of the FAM46C/Plk4/Cep192 complex== | ==Crystal structure of the FAM46C/Plk4/Cep192 complex== | ||
<StructureSection load='6w3j' size='340' side='right'caption='[[6w3j]]' scene=''> | <StructureSection load='6w3j' size='340' side='right'caption='[[6w3j]], [[Resolution|resolution]] 4.38Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6W3J OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6w3j]] is a 3 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=6W3J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6W3J FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.385Å</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=6w3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w3j OCA], [https://pdbe.org/6w3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6w3j RCSB], [https://www.ebi.ac.uk/pdbsum/6w3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6w3j ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/TET5C_HUMAN TET5C_HUMAN] Nucleotidyltransferase that act as a non-canonical poly(A) RNA polymerase which enhances mRNA stability and gene expression. Mainly targets mRNAs encoding endoplasmic reticulum-targeted protein and may be involved in induction of cell death.<ref>PMID:27060136</ref> <ref>PMID:28931820</ref> (Microbial infection) Seems to enhance replication of some viruses, including yellow fever virus, in response to type I interferon.<ref>PMID:21478870</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
FAM46C, a non-canonical poly(A) polymerase, is frequently mutated in multiple myeloma. Loss of function of FAM46C promotes cell survival of multiple myeloma, suggesting a tumor-suppressive role. FAM46C is also essential for fastening sperm head and flagellum, indispensable for male fertility. The molecular mechanisms of these functions of FAM46C remain elusive. We report the crystal structure of FAM46C to provide the basis for its poly(A) polymerase activity and rationalize mutations associated with multiple myeloma. In addition, we found that FAM46C interacts directly with the serine/threonine kinase Plk4, the master regulator of centrosome duplication. We present the structure of FAM46C in complex with the Cryptic Polo-Box 1-2 domains of Plk4. Our structure-based mutational analyses show that the interaction with Plk4 recruits FAM46C to centrosomes. Our data suggest that Plk4-mediated localization of FAM46C enables its regulation of centrosome structure and functions, which may underlie the roles for FAM46C in cell proliferation and sperm development. | |||
Structural and Functional Analyses of the FAM46C/Plk4 Complex.,Chen H, Lu D, Shang G, Gao G, Zhang X Structure. 2020 May 12. pii: S0969-2126(20)30169-6. doi:, 10.1016/j.str.2020.04.023. PMID:32433990<ref>PMID:32433990</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6w3j" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chen H]] | [[Category: Chen H]] | ||
Latest revision as of 17:16, 18 October 2023
Crystal structure of the FAM46C/Plk4/Cep192 complexCrystal structure of the FAM46C/Plk4/Cep192 complex
Structural highlights
FunctionTET5C_HUMAN Nucleotidyltransferase that act as a non-canonical poly(A) RNA polymerase which enhances mRNA stability and gene expression. Mainly targets mRNAs encoding endoplasmic reticulum-targeted protein and may be involved in induction of cell death.[1] [2] (Microbial infection) Seems to enhance replication of some viruses, including yellow fever virus, in response to type I interferon.[3] Publication Abstract from PubMedFAM46C, a non-canonical poly(A) polymerase, is frequently mutated in multiple myeloma. Loss of function of FAM46C promotes cell survival of multiple myeloma, suggesting a tumor-suppressive role. FAM46C is also essential for fastening sperm head and flagellum, indispensable for male fertility. The molecular mechanisms of these functions of FAM46C remain elusive. We report the crystal structure of FAM46C to provide the basis for its poly(A) polymerase activity and rationalize mutations associated with multiple myeloma. In addition, we found that FAM46C interacts directly with the serine/threonine kinase Plk4, the master regulator of centrosome duplication. We present the structure of FAM46C in complex with the Cryptic Polo-Box 1-2 domains of Plk4. Our structure-based mutational analyses show that the interaction with Plk4 recruits FAM46C to centrosomes. Our data suggest that Plk4-mediated localization of FAM46C enables its regulation of centrosome structure and functions, which may underlie the roles for FAM46C in cell proliferation and sperm development. Structural and Functional Analyses of the FAM46C/Plk4 Complex.,Chen H, Lu D, Shang G, Gao G, Zhang X Structure. 2020 May 12. pii: S0969-2126(20)30169-6. doi:, 10.1016/j.str.2020.04.023. PMID:32433990[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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