1sro: Difference between revisions
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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=1sro 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=1sro ConSurf]. | ||
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== Publication Abstract from PubMed == | |||
The S1 domain, originally identified in ribosomal protein S1, is found in a large number of RNA-associated proteins. The structure of the S1 RNA-binding domain from the E. coli polynucleotide phosphorylase has been determined using NMR methods and consists of a five-stranded antiparallel beta barrel. Conserved residues on one face of the barrel and adjacent loops form the putative RNA-binding site. The structure of the S1 domain is very similar to that of cold shock protein, suggesting that they are both derived from an ancient nucleic acid-binding protein. Enhanced sequence searches reveal hitherto unidentified S1 domains in RNase E, RNase II, NusA, EMB-5, and other proteins. | |||
The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold.,Bycroft M, Hubbard TJ, Proctor M, Freund SM, Murzin AG Cell. 1997 Jan 24;88(2):235-42. PMID:9008164<ref>PMID:9008164</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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==See Also== | ==See Also== | ||
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | ||
*[[Ribosomal protein S1|Ribosomal protein S1]] | *[[Ribosomal protein S1|Ribosomal protein S1]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||