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| {{STRUCTURE_2g0c| PDB=2g0c | SCENE= }} | | {{STRUCTURE_2g0c| PDB=2g0c | SCENE= }} |
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| '''Structure of the RNA binding domain (residues 404-479) of the Bacillus subtilis YxiN protein'''
| | ===Structure of the RNA binding domain (residues 404-479) of the Bacillus subtilis YxiN protein=== |
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| ==Overview==
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| The YxiN protein of Bacillus subtilis is a member of the DbpA subfamily of prokaryotic DEAD-box RNA helicases. Like DbpA, it binds with high affinity and specificity to segments of 23S ribosomal RNA as short as 32 nucleotides (nt) that include hairpin 92. Several experiments have shown that the 76-residue carboxy-terminal domain of YxiN is responsible for the high-affinity RNA binding. The domain has been crystallized and its structure has been solved to 1.7 Angstroms resolution. The structure reveals an RNA recognition motif (RRM) fold that is found in many eukaryotic RNA binding proteins; the RRM fold was not apparent from the amino acid sequence. The domain has two solvent exposed aromatic residues at sites that correspond to the aromatic residues of the ribonucleoprotein (RNP) motifs RNP1 and RNP2 that are essential for RNA binding in many RRMs. However, mutagenesis of these residues (Tyr404 and Tyr447) to alanine has little effect on RNA affinity, suggesting that the YxiN domain binds target RNAs in a manner that differs from the binding mode commonly found in many eukaryotic RRMs. | | The line below this paragraph, {{ABSTRACT_PUBMED_16611943}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16611943 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16611943}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: McKay, D B.]] | | [[Category: McKay, D B.]] |
| [[Category: Rna recognition motif]] | | [[Category: Rna recognition motif]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:33:07 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:04:07 2008'' |
