3htx: Difference between revisions

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<StructureSection load='3htx' size='340' side='right'caption='[[3htx]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
<StructureSection load='3htx' size='340' side='right'caption='[[3htx]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3htx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HTX FirstGlance]. <br>
<table><tr><td colspan='2'>[[3htx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HTX FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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]] 3.1&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HEN1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></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=3htx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3htx OCA], [https://pdbe.org/3htx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3htx RCSB], [https://www.ebi.ac.uk/pdbsum/3htx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3htx 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=3htx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3htx OCA], [https://pdbe.org/3htx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3htx RCSB], [https://www.ebi.ac.uk/pdbsum/3htx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3htx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/HEN1_ARATH HEN1_ARATH]] Methyltransferase that adds a methyl group to the ribose of the last nucleotide of small RNAs (sRNAs). This protects the 3'-end of sRNAs from uridylation activity and subsequent degradation. Can methylate 3'-end of microRNAs (miRNAs), small interfering RNAs (siRNas) and trans-acting small interfering RNAs (ta-siRNAs). Involved in plant development through its role in small RNAs processing. Required for the specification of reproductive organ identities and the probable repression of A class genes. May control floral determinacy possibly by regulating the expression of the C class floral homeotic gene AGAMOUS (AG).<ref>PMID:11874905</ref> <ref>PMID:11917084</ref> <ref>PMID:15705854</ref> <ref>PMID:16111943</ref>
[https://www.uniprot.org/uniprot/HEN1_ARATH HEN1_ARATH] Methyltransferase that adds a methyl group to the ribose of the last nucleotide of small RNAs (sRNAs). This protects the 3'-end of sRNAs from uridylation activity and subsequent degradation. Can methylate 3'-end of microRNAs (miRNAs), small interfering RNAs (siRNas) and trans-acting small interfering RNAs (ta-siRNAs). Involved in plant development through its role in small RNAs processing. Required for the specification of reproductive organ identities and the probable repression of A class genes. May control floral determinacy possibly by regulating the expression of the C class floral homeotic gene AGAMOUS (AG).<ref>PMID:11874905</ref> <ref>PMID:11917084</ref> <ref>PMID:15705854</ref> <ref>PMID:16111943</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3htx ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3htx ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
RNA silencing is a conserved regulatory mechanism in fungi, plants and animals that regulates gene expression and defence against viruses and transgenes. Small silencing RNAs of approximately 20-30 nucleotides and their associated effector proteins, the Argonaute family proteins, are the central components in RNA silencing. A subset of small RNAs, such as microRNAs and small interfering RNAs (siRNAs) in plants, Piwi-interacting RNAs in animals and siRNAs in Drosophila, requires an additional crucial step for their maturation; that is, 2'-O-methylation on the 3' terminal nucleotide. A conserved S-adenosyl-l-methionine-dependent RNA methyltransferase, HUA ENHANCER 1 (HEN1), and its homologues are responsible for this specific modification. Here we report the 3.1 A crystal structure of full-length HEN1 from Arabidopsis in complex with a 22-nucleotide small RNA duplex and cofactor product S-adenosyl-l-homocysteine. Highly cooperative recognition of the small RNA substrate by multiple RNA binding domains and the methyltransferase domain in HEN1 measures the length of the RNA duplex and determines the substrate specificity. Metal ion coordination by both 2' and 3' hydroxyls on the 3'-terminal nucleotide and four invariant residues in the active site of the methyltransferase domain suggests a novel Mg(2+)-dependent 2'-O-methylation mechanism.
Structural insights into mechanisms of the small RNA methyltransferase HEN1.,Huang Y, Ji L, Huang Q, Vassylyev DG, Chen X, Ma JB Nature. 2009 Oct 8;461(7265):823-7. PMID:19812675<ref>PMID:19812675</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3htx" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Arath]]
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chen, X M]]
[[Category: Chen X-M]]
[[Category: Huang, Q C]]
[[Category: Huang Q-C]]
[[Category: Huang, Y]]
[[Category: Huang Y]]
[[Category: Ji, L J]]
[[Category: Ji L-J]]
[[Category: Ma, J B]]
[[Category: Ma J-B]]
[[Category: Vassylyev, D G]]
[[Category: Vassylyev DG]]
[[Category: Hen1]]
[[Category: Protein-rna complex]]
[[Category: Sam binding protein]]
[[Category: Small rna methyltransferase]]
[[Category: Transferase-rna complex]]
Retrieved from "https://proteopedia.org/3htx"