2i82
From Proteopedia
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|PDB= 2i82 |SIZE=350|CAPTION= <scene name='initialview01'>2i82</scene>, resolution 2.05Å | |PDB= 2i82 |SIZE=350|CAPTION= <scene name='initialview01'>2i82</scene>, resolution 2.05Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FOU:(5S,6R)-5-FLUORO-6-HYDROXYDIHYDROPYRIMIDINE-2,4(1H,3H)-DIONE'>FOU</scene> | + | |LIGAND= <scene name='pdbligand=A:ADENOSINE-5'-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5'-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=FOU:(5S,6R)-5-FLUORO-6-HYDROXYDIHYDROPYRIMIDINE-2,4(1H,3H)-DIONE'>FOU</scene>, <scene name='pdbligand=G:GUANOSINE-5'-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=N:ANY+5'-MONOPHOSPHATE+NUCLEOTIDE'>N</scene>, <scene name='pdbligand=U:URIDINE-5'-MONOPHOSPHATE'>U</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Pseudouridylate_synthase Pseudouridylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.70 4.2.1.70] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Pseudouridylate_synthase Pseudouridylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.70 4.2.1.70] </span> |
|GENE= rluA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= rluA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i82 OCA], [http://www.ebi.ac.uk/pdbsum/2i82 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i82 RCSB]</span> | ||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hoang, C.]] | [[Category: Hoang, C.]] | ||
| - | [[Category: FOU]] | ||
[[Category: pseudouridine synthase]] | [[Category: pseudouridine synthase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:40:56 2008'' |
Revision as of 00:40, 31 March 2008
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| , resolution 2.05Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , , | ||||||
| Gene: | rluA (Escherichia coli) | ||||||
| Activity: | Pseudouridylate synthase, with EC number 4.2.1.70 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of pseudouridine synthase RluA: indirect sequence readout through protein-induced RNA structure
Overview
RluA is a dual-specificity enzyme responsible for pseudouridylating 23S rRNA and several tRNAs. The 2.05 A resolution structure of RluA bound to a substrate RNA comprising the anticodon stem loop of tRNA(Phe) reveals that enzyme binding induces a dramatic reorganization of the RNA. Instead of adopting its canonical U turn conformation, the anticodon loop folds into a new structure with a reverse-Hoogsteen base pair and three flipped-out nucleotides. Sequence conservation, the cocrystal structure, and the results of structure-guided mutagenesis suggest that RluA recognizes its substrates indirectly by probing RNA loops for their ability to adopt the reorganized fold. The planar, cationic side chain of an arginine intercalates between the reverse-Hoogsteen base pair and the bottom pair of the anticodon stem, flipping the nucleotide to be modified into the active site of RluA. Sequence and structural comparisons suggest that pseudouridine synthases of the RluA, RsuA, and TruA families employ an equivalent arginine for base flipping.
About this Structure
2I82 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of pseudouridine synthase RluA: indirect sequence readout through protein-induced RNA structure., Hoang C, Chen J, Vizthum CA, Kandel JM, Hamilton CS, Mueller EG, Ferre-D'Amare AR, Mol Cell. 2006 Nov 17;24(4):535-45. PMID:17188032
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