1buj
From Proteopedia
(New page: 200px<br /><applet load="1buj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1buj" /> '''STRUCTURE OF BINASE IN SOLUTION'''<br /> ==...) |
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| - | [[Image:1buj.jpg|left|200px]]<br /><applet load="1buj" size=" | + | [[Image:1buj.jpg|left|200px]]<br /><applet load="1buj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1buj" /> | caption="1buj" /> | ||
'''STRUCTURE OF BINASE IN SOLUTION'''<br /> | '''STRUCTURE OF BINASE IN SOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We present the spatial structure of binase, a small extracellular | + | We present the spatial structure of binase, a small extracellular ribonuclease, derived from 1H-NMR* data in aqueous solution. The total of 20 structures were obtained via torsion angle dynamics using DYANA program with experimental NOE and hydrogen bond distance constraints and phi and chi1 dihedral angle constraints. The final structures were energy minimised with ECEPP/2 potential in FANTOM program. Binase consists of three alpha-helices in N-terminal part (residues 6-16, 26-32 and 41-44), five-stranded antiparallel beta-sheet in C-terminal part (residues 51-55, 70-75, 86-90, 94-99 and 104-108) and two-stranded parallel beta-sheet (residues 22-24 and 49-51). Three loops (residues 36-39, 56-67 and 76-83), which play significant role in biological functioning of binase, are flexible in solution. The differences between binase and barnase spatial structures in solution explain the differences in thermostability of binase, barnase and their hybrids. |
==About this Structure== | ==About this Structure== | ||
| - | 1BUJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_intermedius Bacillus intermedius]. Full crystallographic information is available from [http:// | + | 1BUJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_intermedius Bacillus intermedius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BUJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus intermedius]] | [[Category: Bacillus intermedius]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Arseniev, A | + | [[Category: Arseniev, A S.]] |
| - | [[Category: Nolde, D | + | [[Category: Nolde, D E.]] |
| - | [[Category: Reibarkh, M | + | [[Category: Reibarkh, M Y.]] |
| - | [[Category: Vasilieva, L | + | [[Category: Vasilieva, L I.]] |
[[Category: microbial ribonuclease]] | [[Category: microbial ribonuclease]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:16 2008'' |
Revision as of 09:59, 21 February 2008
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STRUCTURE OF BINASE IN SOLUTION
Overview
We present the spatial structure of binase, a small extracellular ribonuclease, derived from 1H-NMR* data in aqueous solution. The total of 20 structures were obtained via torsion angle dynamics using DYANA program with experimental NOE and hydrogen bond distance constraints and phi and chi1 dihedral angle constraints. The final structures were energy minimised with ECEPP/2 potential in FANTOM program. Binase consists of three alpha-helices in N-terminal part (residues 6-16, 26-32 and 41-44), five-stranded antiparallel beta-sheet in C-terminal part (residues 51-55, 70-75, 86-90, 94-99 and 104-108) and two-stranded parallel beta-sheet (residues 22-24 and 49-51). Three loops (residues 36-39, 56-67 and 76-83), which play significant role in biological functioning of binase, are flexible in solution. The differences between binase and barnase spatial structures in solution explain the differences in thermostability of binase, barnase and their hybrids.
About this Structure
1BUJ is a Single protein structure of sequence from Bacillus intermedius. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of binase in solution., Reibarkh MYa, Nolde DE, Vasilieva LI, Bocharov EV, Shulga AA, Kirpichnikov MP, Arseniev AS, FEBS Lett. 1998 Jul 17;431(2):250-4. PMID:9708913
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