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| | ==BARNASE== | | ==BARNASE== |
| - | <StructureSection load='1bnr' size='340' side='right'caption='[[1bnr]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1bnr' size='340' side='right'caption='[[1bnr]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1bnr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_amyloliquifaciens"_(sic)_fukumoto_1943 "bacillus amyloliquifaciens" (sic) fukumoto 1943]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BNR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1BNR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1bnr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BNR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BNR FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BARNASE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1390 "Bacillus amyloliquifaciens" (sic) Fukumoto 1943])</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'>[http://proteopedia.org/fgij/fg.htm?mol=1bnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bnr OCA], [http://pdbe.org/1bnr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bnr RCSB], [http://www.ebi.ac.uk/pdbsum/1bnr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bnr ProSAT]</span></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=1bnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bnr OCA], [https://pdbe.org/1bnr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bnr RCSB], [https://www.ebi.ac.uk/pdbsum/1bnr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bnr ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RNBR_BACAM RNBR_BACAM]] Hydrolyzes phosphodiester bonds in RNA, poly- and oligoribonucleotides resulting in 3'-nucleoside monophosphates via 2',3'-cyclophosphate intermediates. | + | [https://www.uniprot.org/uniprot/RNBR_BACAM RNBR_BACAM] Hydrolyzes phosphodiester bonds in RNA, poly- and oligoribonucleotides resulting in 3'-nucleoside monophosphates via 2',3'-cyclophosphate intermediates. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | *[[Barnase 3D structures|Barnase 3D structures]] | | *[[Barnase 3D structures|Barnase 3D structures]] |
| | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] |
| - | *[[Temp|Temp]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Bacillus amyloliquefaciens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bycroft, M]] | + | [[Category: Bycroft M]] |
| - | [[Category: Microbial ribonuclease]]
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| Structural highlights
Function
RNBR_BACAM Hydrolyzes phosphodiester bonds in RNA, poly- and oligoribonucleotides resulting in 3'-nucleoside monophosphates via 2',3'-cyclophosphate intermediates.
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 solution conformation of the ribonuclease barnase has been determined by using 1H nuclear magnetic resonance (NMR) spectroscopy. The 20 structures were calculated by using 853 interproton distance restraints obtained from analyses of two-dimensional nuclear Overhauser spectra, 72 phi and 53 chi 1 torsion angle restraints, and 17 hydrogen-bond distance restraints. The calculated structures contain two alpha-helices (residues 6-18 and 26-34) and a five-stranded antiparallel beta-sheet (residues 50-55, 70-75, 85-91, 94-101, and 105-108). The core of the protein is formed by the packing of one of the alpha-helices (residues 6-18) onto the beta-sheet. The average RMS deviation between the calculated structures and the mean structure is 1.11 A for the backbone atoms and 1.75 A for all atoms. The protein is least well-defined in the N-terminal region and in three large loops. When these regions are excluded, the average RMS deviation between the calculated structures and the mean structure for residues 5-34, 50-56, 71-76, 85-109 is 0.62 A for the backbone atoms and 1.0 A for all atoms. The NMR-derived structure has been compared with the crystal structure of barnase [Mauguen et al. (1982) Nature (London) 297, 162-164].
Determination of the three-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy.,Bycroft M, Ludvigsen S, Fersht AR, Poulsen FM Biochemistry. 1991 Sep 3;30(35):8697-701. PMID:1888730[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bycroft M, Ludvigsen S, Fersht AR, Poulsen FM. Determination of the three-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy. Biochemistry. 1991 Sep 3;30(35):8697-701. PMID:1888730
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