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| | <StructureSection load='1b21' size='340' side='right'caption='[[1b21]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1b21' size='340' side='right'caption='[[1b21]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1b21]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_amyloliquifaciens"_(sic)_fukumoto_1943 "bacillus amyloliquifaciens" (sic) fukumoto 1943]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B21 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B21 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1b21]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B21 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B21 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1b21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b21 OCA], [https://pdbe.org/1b21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b21 RCSB], [https://www.ebi.ac.uk/pdbsum/1b21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b21 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=1b21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b21 OCA], [https://pdbe.org/1b21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b21 RCSB], [https://www.ebi.ac.uk/pdbsum/1b21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b21 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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.
| + | [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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Bacillus amyloliquefaciens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Buckle, A M]] | + | [[Category: Buckle AM]] |
| - | [[Category: Fersht, A R]] | + | [[Category: Fersht AR]] |
| - | [[Category: Harryson, P]] | + | [[Category: Harryson P]] |
| - | [[Category: Oliveberg, M]] | + | [[Category: Oliveberg M]] |
| - | [[Category: Vaughan, C K]] | + | [[Category: Vaughan CK]] |
| - | [[Category: Alpha/beta protein]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Microbial ribonuclease]]
| + | |
| 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
Double-mutant cycles are widely used in the field of protein engineering to measure intermolecular and intramolecular interactions. Ideally, there should be no structural rearrangement of the protein on making the two single mutations and the double mutation within the cycle. However, structural pertubation on mutation does not preclude the use of this method, providing the sum of the changes in the single mutants equals the change in the double mutant. In this way, the energy associated with any structural rearrangement cancels in the double-mutant cycle. Previously, the contribution of a buried salt bridge between Arg69 and Asp93 in barnase to the stability of the folded protein has been determined by double-mutant cycle analysis. In order to determine whether the measured interaction of -14.0 kJ mol(-1) represents the true interaction energy, the crystal structure of each mutant within the double-mutant cycle was solved. Although mutation results in structural shifts, the majority of those in the single mutants are also found in the double mutant; their energetic effects in the double-mutant cycle are therefore cancelled. This study highlights the robust nature of the double-mutant cycle analysis.
A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase.,Vaughan CK, Harryson P, Buckle AM, Fersht AR Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):591-600. Epub 2002, Mar 22. PMID:11914482[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Vaughan CK, Harryson P, Buckle AM, Fersht AR. A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase. Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):591-600. Epub 2002, Mar 22. PMID:11914482
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