1sro

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{{STRUCTURE_1sro| PDB=1sro | SCENE= }}
{{STRUCTURE_1sro| PDB=1sro | SCENE= }}
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'''S1 RNA BINDING DOMAIN, NMR, 20 STRUCTURES'''
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===S1 RNA BINDING DOMAIN, NMR, 20 STRUCTURES===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_9008164}}
==About this Structure==
==About this Structure==
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1SRO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SRO OCA].
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1SRO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SRO OCA].
==Reference==
==Reference==
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[[Category: Bycroft, M.]]
[[Category: Bycroft, M.]]
[[Category: S1 rna-binding domain]]
[[Category: S1 rna-binding domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:13:29 2008''

Revision as of 17:13, 27 July 2008

Image:1sro.png

Template:STRUCTURE 1sro

S1 RNA BINDING DOMAIN, NMR, 20 STRUCTURES

Template:ABSTRACT PUBMED 9008164

About this Structure

1SRO is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

Reference

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

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