6w3j: Difference between revisions

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<StructureSection load='6w3j' size='340' side='right'caption='[[6w3j]], [[Resolution|resolution]] 4.38&Aring;' scene=''>
<StructureSection load='6w3j' size='340' side='right'caption='[[6w3j]], [[Resolution|resolution]] 4.38&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6w3j]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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>
<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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TENT5C, FAM46C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PLK4, SAK, STK18 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CEP192, KIAA1569, PP8407 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 4.385&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Polynucleotide_adenylyltransferase Polynucleotide adenylyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.19 2.7.7.19] </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=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>
<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 ==
== 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> [[https://www.uniprot.org/uniprot/CE192_HUMAN CE192_HUMAN]] Required for mitotic centrosome maturation and bipolar spindle assembly (PubMed:25042804, PubMed:17980596, PubMed:18207742). Appears to be a major regulator of pericentriolar material (PCM) recruitment, centrosome maturation, and centriole duplication (PubMed:25042804, PubMed:17980596, PubMed:18207742). Centrosome-specific activating scaffold for AURKA and PLK1 (PubMed:25042804).<ref>PMID:17980596</ref> <ref>PMID:18207742</ref> <ref>PMID:25042804</ref>  [[https://www.uniprot.org/uniprot/PLK4_HUMAN PLK4_HUMAN]] Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition, leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Phosphorylates CDC25C and CHEK2.<ref>PMID:16326102</ref> <ref>PMID:16244668</ref> <ref>PMID:17681131</ref> <ref>PMID:18239451</ref> <ref>PMID:19164942</ref> <ref>PMID:21725316</ref> 
[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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Polynucleotide adenylyltransferase]]
[[Category: Chen H]]
[[Category: Chen, H]]
[[Category: Lu DF]]
[[Category: Lu, D F]]
[[Category: Shang GJ]]
[[Category: Shang, G J]]
[[Category: Zhang XW]]
[[Category: Zhang, X W]]
[[Category: Rna polymerase]]
[[Category: Transferase]]

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

6w3j is a 3 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 4.385Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[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 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[4]

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

See Also

References

  1. ↑ Kuchta K, Muszewska A, Knizewski L, Steczkiewicz K, Wyrwicz LS, Pawlowski K, Rychlewski L, Ginalski K. FAM46 proteins are novel eukaryotic non-canonical poly(A) polymerases. Nucleic Acids Res. 2016 May 5;44(8):3534-48. doi: 10.1093/nar/gkw222. Epub 2016, Apr 7. PMID:27060136 doi:http://dx.doi.org/10.1093/nar/gkw222
  2. ↑ Mroczek S, Chlebowska J, Kulinski TM, Gewartowska O, Gruchota J, Cysewski D, Liudkovska V, Borsuk E, Nowis D, Dziembowski A. The non-canonical poly(A) polymerase FAM46C acts as an onco-suppressor in multiple myeloma. Nat Commun. 2017 Sep 20;8(1):619. doi: 10.1038/s41467-017-00578-5. PMID:28931820 doi:http://dx.doi.org/10.1038/s41467-017-00578-5
  3. ↑ Schoggins JW, Wilson SJ, Panis M, Murphy MY, Jones CT, Bieniasz P, Rice CM. A diverse range of gene products are effectors of the type I interferon antiviral response. Nature. 2011 Apr 28;472(7344):481-5. doi: 10.1038/nature09907. Epub 2011 Apr 10. PMID:21478870 doi:10.1038/nature09907
  4. ↑ Chen H, Lu D, Shang G, Gao G, Zhang X. Structural and Functional Analyses of the FAM46C/Plk4 Complex. Structure. 2020 May 12. pii: S0969-2126(20)30169-6. doi:, 10.1016/j.str.2020.04.023. PMID:32433990 doi:http://dx.doi.org/10.1016/j.str.2020.04.023

6w3j, resolution 4.38Å

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