1a19
From Proteopedia
(New page: 200px<br /><applet load="1a19" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a19, resolution 2.76Å" /> '''BARSTAR (FREE), C82A...) |
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| - | [[Image:1a19.gif|left|200px]]<br /><applet load="1a19" size=" | + | [[Image:1a19.gif|left|200px]]<br /><applet load="1a19" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1a19, resolution 2.76Å" /> | caption="1a19, resolution 2.76Å" /> | ||
'''BARSTAR (FREE), C82A MUTANT'''<br /> | '''BARSTAR (FREE), C82A MUTANT'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the C82A mutant of barstar, the intracellular | + | The 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1A19 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http:// | + | 1A19 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://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]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus amyloliquefaciens]] | [[Category: Bacillus amyloliquefaciens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Ratnaparkhi, G | + | [[Category: Ratnaparkhi, G S.]] |
[[Category: Varadarajan, R.]] | [[Category: Varadarajan, R.]] | ||
[[Category: barstar]] | [[Category: barstar]] | ||
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[[Category: uncomplexed]] | [[Category: uncomplexed]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:44 2008'' |
Revision as of 09:39, 21 February 2008
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BARSTAR (FREE), C82A MUTANT
Overview
The 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.
About this Structure
1A19 is a Single protein structure of sequence from Bacillus amyloliquefaciens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 11:39:44 2008
