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| | ==THREE-DIMENSIONAL SOLUTION STRUCTURE AND 13C ASSIGNMENTS OF BARSTAR USING NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY== | | ==THREE-DIMENSIONAL SOLUTION STRUCTURE AND 13C ASSIGNMENTS OF BARSTAR USING NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY== |
| - | <StructureSection load='1btb' size='340' side='right'caption='[[1btb]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | + | <StructureSection load='1btb' size='340' side='right'caption='[[1btb]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1btb]] 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=1BTB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BTB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1btb]] 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=1BTB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BTB FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bta|1bta]]</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1btb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btb OCA], [http://pdbe.org/1btb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1btb RCSB], [http://www.ebi.ac.uk/pdbsum/1btb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1btb 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=1btb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btb OCA], [https://pdbe.org/1btb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1btb RCSB], [https://www.ebi.ac.uk/pdbsum/1btb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1btb ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BARS_BACAM BARS_BACAM]] Inhibitor of the ribonuclease barnase. Forms a one-to-one non-covalent complex. | + | [https://www.uniprot.org/uniprot/BARS_BACAM BARS_BACAM] Inhibitor of the ribonuclease barnase. Forms a one-to-one non-covalent complex. |
| | == 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: Bycroft, M]] | + | [[Category: Bycroft M]] |
| - | [[Category: Fersht, A R]] | + | [[Category: Fersht AR]] |
| - | [[Category: Freund, S M.V]] | + | [[Category: Freund SMV]] |
| - | [[Category: Lubienski, M J]] | + | [[Category: Lubienski MJ]] |
| - | [[Category: Ribonuclease inhibitor]]
| + | |
| Structural highlights
Function
BARS_BACAM Inhibitor of the ribonuclease barnase. Forms a one-to-one non-covalent complex.
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
We present the high-resolution solution structure and 13C assignments of wild-type barstar, an 89 amino acid residue polypeptide inhibitor of barnase, derived from heteronuclear NMR techniques. These were obtained from measurements on unlabeled, uniformly 15N- and 13C/15N-labeled, and 10% 13C-labeled barstar samples that have both cysteines (at positions 40 and 82) fully reduced. In total, 30 structures were calculated by hybrid distance geometry-dynamical simulated annealing calculations. The atomic rms distribution about the mean coordinate positions is 0.42 A for all backbone atoms and 0.90 A for all atoms. The structure is composed of three parallel alpha-helices packed against a three-stranded parallel beta-sheet. A more poorly defined helix links the second beta-strand and the third major alpha-helix. The loop involved in binding barnase is extremely well defined and held rigidly by interactions from the main body of the protein to both ends and the middle of the loop. This structure will be used to aid protein engineering studies currently taking place on the free and bound states of barstar and barnase.
Three-dimensional solution structure and 13C assignments of barstar using nuclear magnetic resonance spectroscopy.,Lubienski MJ, Bycroft M, Freund SM, Fersht AR Biochemistry. 1994 Aug 2;33(30):8866-77. PMID:8043574[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lubienski MJ, Bycroft M, Freund SM, Fersht AR. Three-dimensional solution structure and 13C assignments of barstar using nuclear magnetic resonance spectroscopy. Biochemistry. 1994 Aug 2;33(30):8866-77. PMID:8043574
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