1a19: Difference between revisions
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<StructureSection load='1a19' size='340' side='right'caption='[[1a19]], [[Resolution|resolution]] 2.76Å' scene=''> | <StructureSection load='1a19' size='340' side='right'caption='[[1a19]], [[Resolution|resolution]] 2.76Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1a19]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1a19]] is a 2 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=1A19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A19 FirstGlance]. <br> | ||
</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=1a19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a19 OCA], [https://pdbe.org/1a19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a19 RCSB], [https://www.ebi.ac.uk/pdbsum/1a19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a19 ProSAT]</span></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]] 2.76Å</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=1a19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a19 OCA], [https://pdbe.org/1a19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a19 RCSB], [https://www.ebi.ac.uk/pdbsum/1a19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a19 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[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: Ratnaparkhi | [[Category: Ratnaparkhi GS]] | ||
[[Category: Varadarajan | [[Category: Varadarajan R]] | ||
Latest revision as of 13:44, 2 August 2023
BARSTAR (FREE), C82A MUTANTBARSTAR (FREE), C82A MUTANT
Structural highlights
FunctionBARS_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 PubMedThe crystal structure of the C82A mutant of barstar, the intracellular inhibitor of the Bacillus amyloliquefaciens ribonuclease barnase, has been solved to a resolution of 2.8 A. The molecule crystallizes in the space group I41 with a dimer in the asymmetric unit. An identical barstar dimer is also found in the crystal structure of the barnase-barstar complex. This structure of uncomplexed barstar is compared to the structure of barstar bound to barnase and also to the structure of barstar solved using NMR. The free structure is similar to the bound state, and there are no significant main-chain differences in the 27-44 region involved in barstar binding to barnase. The C82A structure shows significant differences from the average NMR structure, both overall and in the binding region. In contrast to the crystal structure, the NMR structure shows an unusually high packing value based on the occluded surface algorithm, indicating errors in the packing of the structure. We show that the NMR structures of homologous proteins generally show large differences in packing value, while the crystal structures of such proteins have very similar packing values, suggesting that protein packing density is not well determined by NMR. Discrepancies between the NMR and X-ray structures of uncomplexed barstar: analysis suggests that packing densities of protein structures determined by NMR are unreliable.,Ratnaparkhi GS, Ramachandran S, Udgaonkar JB, Varadarajan R Biochemistry. 1998 May 12;37(19):6958-66. PMID:9578582[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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