6uca

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<StructureSection load='6uca' size='340' side='right'caption='[[6uca]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
<StructureSection load='6uca' size='340' side='right'caption='[[6uca]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6uca]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UCA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6UCA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6uca]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UCA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6UCA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ZCCHC4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ZCCHC4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<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=6uca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uca OCA], [http://pdbe.org/6uca PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6uca RCSB], [http://www.ebi.ac.uk/pdbsum/6uca PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6uca ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6uca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uca OCA], [http://pdbe.org/6uca PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6uca RCSB], [http://www.ebi.ac.uk/pdbsum/6uca PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6uca ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ZCHC4_HUMAN ZCHC4_HUMAN]] rRNA N6-methyltransferase that specifically methylates the adenine in position 4220 of 28S rRNA (PubMed:30531910). N6-methylation of adenine(4220) in 28S rRNA is required for translation (PubMed:30531910).<ref>PMID:30531910</ref>
[[http://www.uniprot.org/uniprot/ZCHC4_HUMAN ZCHC4_HUMAN]] rRNA N6-methyltransferase that specifically methylates the adenine in position 4220 of 28S rRNA (PubMed:30531910). N6-methylation of adenine(4220) in 28S rRNA is required for translation (PubMed:30531910).<ref>PMID:30531910</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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N(6)-methyladenosine (m(6)A) modification provides an important epitranscriptomic mechanism that critically regulates RNA metabolism and function. However, how m(6)A writers attain substrate specificities remains unclear. We report the 3.1 A-resolution crystal structure of human CCHC zinc finger-containing protein ZCCHC4, a 28S rRNA-specific m(6)A methyltransferase, bound to S-adenosyl-L-homocysteine. The methyltransferase (MTase) domain of ZCCHC4 is packed against N-terminal GRF-type and C2H2 zinc finger domains and a C-terminal CCHC domain, creating an integrated RNA-binding surface. Strikingly, the MTase domain adopts an autoinhibitory conformation, with a self-occluded catalytic site and a fully-closed cofactor pocket. Mutational and enzymatic analyses further substantiate the molecular basis for ZCCHC4-RNA recognition and a role of the stem-loop structure within substrate in governing the substrate specificity. Overall, this study unveils unique structural and enzymatic characteristics of ZCCHC4, distinctive from what was seen with the METTL family of m(6)A writers, providing the mechanistic basis for ZCCHC4 modulation of m(6)A RNA methylation.
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Structure and regulation of ZCCHC4 in m(6)A-methylation of 28S rRNA.,Ren W, Lu J, Huang M, Gao L, Li D, Wang GG, Song J Nat Commun. 2019 Nov 6;10(1):5042. doi: 10.1038/s41467-019-12923-x. PMID:31695039<ref>PMID:31695039</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6uca" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Revision as of 07:12, 29 April 2020

Crystal structure of human ZCCHC4 in complex with SAH

PDB ID 6uca

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