2ab5: Difference between revisions

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==bI3 LAGLIDADG Maturase==
==bI3 LAGLIDADG Maturase==
<StructureSection load='2ab5' size='340' side='right' caption='[[2ab5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='2ab5' size='340' side='right'caption='[[2ab5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ab5]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AB5 FirstGlance]. <br>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.2&#8491;</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='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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cytochrome b intron bi3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</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>
<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=2ab5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ab5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ab5 RCSB], [http://www.ebi.ac.uk/pdbsum/2ab5 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ab/2ab5_consurf.spt"</scriptWhenChecked>
     <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/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata 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=2ab5 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 2ab5" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Bassi, G S]]
[[Category: Bassi GS]]
[[Category: Berndt, D]]
[[Category: Berndt D]]
[[Category: Hall, T M]]
[[Category: Hall TM]]
[[Category: Krahn, J M]]
[[Category: Krahn JM]]
[[Category: Leonard, C W]]
[[Category: Leonard CW]]
[[Category: Longo, A]]
[[Category: Longo A]]
[[Category: Weeks, K M]]
[[Category: Weeks KM]]
[[Category: Group i intron splicing]]
[[Category: Laglidadg endonuclease]]
[[Category: Maturase]]
[[Category: Protein binding]]
[[Category: Rna binding]]

Latest revision as of 10:48, 30 October 2024

bI3 LAGLIDADG MaturasebI3 LAGLIDADG Maturase

Structural highlights

2ab5 is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2]

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 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.

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[3]

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

See Also

References

  1. Bassi GS, de Oliveira DM, White MF, Weeks KM. Recruitment of intron-encoded and co-opted proteins in splicing of the bI3 group I intron RNA. Proc Natl Acad Sci U S A. 2002 Jan 8;99(1):128-33. Epub 2002 Jan 2. PMID:11773622 doi:http://dx.doi.org/10.1073/pnas.012579299
  2. Bassi GS, Weeks KM. Kinetic and thermodynamic framework for assembly of the six-component bI3 group I intron ribonucleoprotein catalyst. Biochemistry. 2003 Aug 26;42(33):9980-8. PMID:12924947 doi:http://dx.doi.org/10.1021/bi0346906
  3. Longo A, Leonard CW, Bassi GS, Berndt D, Krahn JM, Hall TM, Weeks KM. Evolution from DNA to RNA recognition by the bI3 LAGLIDADG maturase. Nat Struct Mol Biol. 2005 Sep;12(9):779-87. Epub 2005 Aug 21. PMID:16116439 doi:http://dx.doi.org/10.1038/nsmb976

2ab5, resolution 2.20Å

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