2ab5: Difference between revisions
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== | ==bI3 LAGLIDADG Maturase== | ||
<StructureSection load='2ab5' size='340' side='right'caption='[[2ab5]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2ab5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AB5 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2ab5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ab5 OCA], [https://pdbe.org/2ab5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ab5 RCSB], [https://www.ebi.ac.uk/pdbsum/2ab5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ab5 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MBI3_YEAST MBI3_YEAST] Mitochondrial mRNA maturase required for splicing of intron 3 of the cytochrome b (COB) gene, containing its own coding sequence. In vivo splicing requires the formation of a ribonucleoprotein complex together with the imported mitochondrial RNA-splicing protein MRS1. The complex seems to stimulate the intrinsic ribozyme activity of intron bI3 through binding to and stabilizing specific secondary and tertiary structure elements in the RNA.<ref>PMID:11773622</ref> <ref>PMID:12924947</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/ab/2ab5_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2ab5 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
LAGLIDADG endonucleases bind across adjacent major grooves via a saddle-shaped surface and catalyze DNA cleavage. Some LAGLIDADG proteins, called maturases, facilitate splicing by group I introns, raising the issue of how a DNA-binding protein and an RNA have evolved to function together. In this report, crystallographic analysis shows that the global architecture of the bI3 maturase is unchanged from its DNA-binding homologs; in contrast, the endonuclease active site, dispensable for splicing facilitation, is efficiently compromised by a lysine residue replacing essential catalytic groups. Biochemical experiments show that the maturase binds a peripheral RNA domain 50 A from the splicing active site, exemplifying long-distance structural communication in a ribonucleoprotein complex. The bI3 maturase nucleic acid recognition saddle interacts at the RNA minor groove; thus, evolution from DNA to RNA function has been mediated by a switch from major to minor groove interaction. | LAGLIDADG endonucleases bind across adjacent major grooves via a saddle-shaped surface and catalyze DNA cleavage. Some LAGLIDADG proteins, called maturases, facilitate splicing by group I introns, raising the issue of how a DNA-binding protein and an RNA have evolved to function together. In this report, crystallographic analysis shows that the global architecture of the bI3 maturase is unchanged from its DNA-binding homologs; in contrast, the endonuclease active site, dispensable for splicing facilitation, is efficiently compromised by a lysine residue replacing essential catalytic groups. Biochemical experiments show that the maturase binds a peripheral RNA domain 50 A from the splicing active site, exemplifying long-distance structural communication in a ribonucleoprotein complex. The bI3 maturase nucleic acid recognition saddle interacts at the RNA minor groove; thus, evolution from DNA to RNA function has been mediated by a switch from major to minor groove interaction. | ||
Evolution from DNA to RNA recognition by the bI3 LAGLIDADG maturase.,Longo A, Leonard CW, Bassi GS, Berndt D, Krahn JM, Hall TM, Weeks KM Nat Struct Mol Biol. 2005 Sep;12(9):779-87. Epub 2005 Aug 21. PMID:16116439<ref>PMID:16116439</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 2ab5" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Non-Standard Residue|Non-Standard Residue]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Bassi GS]] | |||
[[Category: Bassi | [[Category: Berndt D]] | ||
[[Category: Berndt | [[Category: Hall TM]] | ||
[[Category: Hall | [[Category: Krahn JM]] | ||
[[Category: Krahn | [[Category: Leonard CW]] | ||
[[Category: Leonard | [[Category: Longo A]] | ||
[[Category: Longo | [[Category: Weeks KM]] | ||
[[Category: Weeks | |||