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| | ==S1 RNA BINDING DOMAIN, NMR, 20 STRUCTURES== | | ==S1 RNA BINDING DOMAIN, NMR, 20 STRUCTURES== |
| - | <StructureSection load='1sro' size='340' side='right'caption='[[1sro]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1sro' size='340' side='right'caption='[[1sro]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1sro]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SRO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SRO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1sro]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SRO FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sro OCA], [http://pdbe.org/1sro PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sro RCSB], [http://www.ebi.ac.uk/pdbsum/1sro PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sro ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sro OCA], [https://pdbe.org/1sro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sro RCSB], [https://www.ebi.ac.uk/pdbsum/1sro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sro ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PNP_ECOLI PNP_ECOLI]] Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3'- to 5'-direction.[HAMAP-Rule:MF_01595] | + | [https://www.uniprot.org/uniprot/PNP_ECOLI PNP_ECOLI] Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3'- to 5'-direction.[HAMAP-Rule:MF_01595] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bycroft, M]] | + | [[Category: Bycroft M]] |
| - | [[Category: S1 rna-binding domain]]
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| Structural highlights
Function
PNP_ECOLI Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3'- to 5'-direction.[HAMAP-Rule:MF_01595]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bycroft M, Hubbard TJ, Proctor M, Freund SM, Murzin AG. The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold. Cell. 1997 Jan 24;88(2):235-42. PMID:9008164
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