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1rlv

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[[Image:1rlv.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of a dimeric Archaeal Splicing Endonuclease==
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|PDB= 1rlv |SIZE=350|CAPTION= <scene name='initialview01'>1rlv</scene>, resolution 3.00&Aring;
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<StructureSection load='1rlv' size='340' side='right'caption='[[1rlv]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1rlv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RLV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RLV FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/tRNA-intron_endonuclease tRNA-intron endonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.9 3.1.27.9]
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</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&#8491;</td></tr>
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|GENE= ENDA, AF0900 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 Archaeoglobus fulgidus])
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rlv OCA], [https://pdbe.org/1rlv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rlv RCSB], [https://www.ebi.ac.uk/pdbsum/1rlv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rlv ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ENDA_ARCFU ENDA_ARCFU] Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a stem of 4 bp.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rl/1rlv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1rlv ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of a dimeric Archaeal Splicing Endonuclease'''
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==See Also==
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*[[Endonuclease 3D structures|Endonuclease 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The splicing endonuclease from Archaeoglobus fulgidus (AF) belongs to the homodimeric family of splicing endonucleases, thought to have evolved from the homotetrameric endonucleases. We report here the crystal structure of the AF endonuclease determined at 2.8 A. The crystal structure of the full-length AF endonuclease contains a homodimer, with each monomer consisting of two homologous repeats joined together by an extended polypeptide chain of ten amino acid residues. The C-terminal repeat has a strong homology to that of a single subunit of the previously determined homotetrameric tRNA splicing endonuclease from Methanococcus jannaschii (MJ), indicating its role in catalysis. The N-terminal repeat is a more degenerate form of the MJ enzyme. Thus the N-terminal repeat is a "non-active" endonuclease fold evolved from the "active" one. By detailed comparison of the structures of the N-terminal and the C-terminal repeats, the binding region for RNA substrates containing a bulge-helix-bulge motif can be identified. Based on the identified RNA-binding region, a cation-pi interaction is suggested to be responsible for coordinating activities between the two active sites. In addition, the full-length AF endonuclease can adopt a higher-ordered fibrous structure in solution, as revealed by the unusual crystallographic packing interactions and other biochemical analysis. This 4(3)-fold fibrous structure adopted by the full-length enzyme is inaccessible to the RNA substrate and is largely stabilized by the first 60 amino acid residues. A mutated form of AF endonuclease with its first 60 residues removed catalyzes the cleavage reaction at a significantly higher rate. Whether there is any role in vivo for this structure-mediated modulation of activity remains to be determined.
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==About this Structure==
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1RLV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RLV OCA].
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==Reference==
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Crystal structure of a dimeric archaeal splicing endonuclease., Li H, Abelson J, J Mol Biol. 2000 Sep 22;302(3):639-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10986124 10986124]
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[[Category: Archaeoglobus fulgidus]]
[[Category: Archaeoglobus fulgidus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: tRNA-intron endonuclease]]
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[[Category: Abelson J]]
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[[Category: Abelson, J.]]
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[[Category: Li H]]
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[[Category: Li, H.]]
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[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:53:23 2008''
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Current revision

Crystal structure of a dimeric Archaeal Splicing Endonuclease

PDB ID 1rlv

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