2id0: Difference between revisions
Jump to navigation
Jump to search
New page: left|200px<br /><applet load="2id0" size="450" color="white" frame="true" align="right" spinBox="true" caption="2id0, resolution 2.350Å" /> '''Escherichia coli RN... |
No edit summary |
||
| (14 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
== | ==Escherichia coli RNase II== | ||
RNase II is a member of the widely distributed RNR family of | <StructureSection load='2id0' size='340' side='right'caption='[[2id0]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2id0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ID0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ID0 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rnb ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Exoribonuclease_II Exoribonuclease II], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.13.1 3.1.13.1] </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=2id0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2id0 OCA], [https://pdbe.org/2id0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2id0 RCSB], [https://www.ebi.ac.uk/pdbsum/2id0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2id0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[https://www.uniprot.org/uniprot/RNB_ECOLI RNB_ECOLI]] Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction.<ref>PMID:11948193</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/id/2id0_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=2id0 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
RNase II is a member of the widely distributed RNR family of exoribonucleases, which are highly processive 3'-->5' hydrolytic enzymes that play an important role in mRNA decay. Here, we report the crystal structure of E. coli RNase II, which reveals an architecture reminiscent of the RNA exosome. Three RNA-binding domains come together to form a clamp-like assembly, which can only accommodate single-stranded RNA. This leads into a narrow, basic channel that ends at the putative catalytic center that is completely enclosed within the body of the protein. The putative path for RNA agrees well with biochemical data indicating that a 3' single strand overhang of 7-10 nt is necessary for binding and hydrolysis by RNase II. The presence of the clamp and the narrow channel provides an explanation for the processivity of RNase II and for why its action is limited to single-stranded RNA. | |||
Structural basis for processivity and single-strand specificity of RNase II.,Zuo Y, Vincent HA, Zhang J, Wang Y, Deutscher MP, Malhotra A Mol Cell. 2006 Oct 6;24(1):149-56. Epub 2006 Sep 21. PMID:16996291<ref>PMID:16996291</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 2id0" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ecoli]] | |||
[[Category: Exoribonuclease II]] | [[Category: Exoribonuclease II]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Malhotra, A | [[Category: Malhotra, A]] | ||
[[Category: Wang, Y | [[Category: Wang, Y]] | ||
[[Category: Zhang, J | [[Category: Zhang, J]] | ||
[[Category: Zuo, Y | [[Category: Zuo, Y]] | ||
[[Category: | [[Category: Exonuclease]] | ||
[[Category: | [[Category: Exoribonuclease]] | ||
[[Category: | [[Category: Hydrolase]] | ||
[[Category: | [[Category: Hydrolyase]] | ||
[[Category: | [[Category: Mrna decay]] | ||
[[Category: | [[Category: Nuclease]] | ||
[[Category: | [[Category: Ribonuclease]] | ||
[[Category: | [[Category: Rnase]] | ||
[[Category: | [[Category: Rnr family]] | ||
Latest revision as of 14:13, 31 March 2021
Escherichia coli RNase IIEscherichia coli RNase II
Structural highlights
Function[RNB_ECOLI] Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedRNase II is a member of the widely distributed RNR family of exoribonucleases, which are highly processive 3'-->5' hydrolytic enzymes that play an important role in mRNA decay. Here, we report the crystal structure of E. coli RNase II, which reveals an architecture reminiscent of the RNA exosome. Three RNA-binding domains come together to form a clamp-like assembly, which can only accommodate single-stranded RNA. This leads into a narrow, basic channel that ends at the putative catalytic center that is completely enclosed within the body of the protein. The putative path for RNA agrees well with biochemical data indicating that a 3' single strand overhang of 7-10 nt is necessary for binding and hydrolysis by RNase II. The presence of the clamp and the narrow channel provides an explanation for the processivity of RNase II and for why its action is limited to single-stranded RNA. Structural basis for processivity and single-strand specificity of RNase II.,Zuo Y, Vincent HA, Zhang J, Wang Y, Deutscher MP, Malhotra A Mol Cell. 2006 Oct 6;24(1):149-56. Epub 2006 Sep 21. PMID:16996291[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||||