2ab5

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|PDB= 2ab5 |SIZE=350|CAPTION= <scene name='initialview01'>2ab5</scene>, resolution 2.200&Aring;
|PDB= 2ab5 |SIZE=350|CAPTION= <scene name='initialview01'>2ab5</scene>, resolution 2.200&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= cytochrome b intron bi3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
|GENE= cytochrome b intron bi3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<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.ebi.ac.uk/pdbsum/2ab5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ab5 RCSB]</span>
}}
}}
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[[Category: Longo, A.]]
[[Category: Longo, A.]]
[[Category: Weeks, K M.]]
[[Category: Weeks, K M.]]
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[[Category: SO4]]
 
[[Category: group i intron splicing]]
[[Category: group i intron splicing]]
[[Category: laglidadg endonuclease]]
[[Category: laglidadg endonuclease]]
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[[Category: rna binding]]
[[Category: rna binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:47:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:50:20 2008''

Revision as of 22:50, 30 March 2008


PDB ID 2ab5

Drag the structure with the mouse to rotate
, resolution 2.200Å
Ligands: ,
Gene: cytochrome b intron bi3 (Saccharomyces cerevisiae)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



bI3 LAGLIDADG Maturase


Overview

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.

About this Structure

2AB5 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

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

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