1bm9
From Proteopedia
(New page: 200px<br /><applet load="1bm9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bm9, resolution 2.00Å" /> '''REPLICATION TERMINAT...) |
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| - | [[Image:1bm9.jpg|left|200px]]<br /><applet load="1bm9" size=" | + | [[Image:1bm9.jpg|left|200px]]<br /><applet load="1bm9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bm9, resolution 2.00Å" /> | caption="1bm9, resolution 2.00Å" /> | ||
'''REPLICATION TERMINATOR PROTEIN FROM BACILLUS SUBTILIS'''<br /> | '''REPLICATION TERMINATOR PROTEIN FROM BACILLUS SUBTILIS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the replication terminator protein (RTP) of B. | + | The crystal structure of the replication terminator protein (RTP) of B. subtilis has been determined at 2.6 A resolution. As previously suggested by both biochemical and biophysical studies, the molecule exists as a symmetric dimer and is in the alpha + beta protein-folding class. The protein has several uncommon features, including an antiparallel coiled-coil, which serves as the dimerization domain, and both an alpha-helix and a beta-ribbon suitably positioned to interact with the major and minor grooves of B-DNA. A site has been identified on the surface of RTP that is biochemically and positionally suitable for interaction with the replication-specific helicase. Other features of the structure are consistent with the polar contrahelicase mechanism of the protein. A model of the interaction between RTP and its cognate DNA is presented. |
==About this Structure== | ==About this Structure== | ||
| - | 1BM9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http:// | + | 1BM9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BM9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bastia, D.]] | [[Category: Bastia, D.]] | ||
| - | [[Category: Bussiere, D | + | [[Category: Bussiere, D E.]] |
[[Category: White, S.]] | [[Category: White, S.]] | ||
[[Category: contrahelicase]] | [[Category: contrahelicase]] | ||
[[Category: dna-binding protein]] | [[Category: dna-binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:56:46 2008'' |
Revision as of 09:56, 21 February 2008
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REPLICATION TERMINATOR PROTEIN FROM BACILLUS SUBTILIS
Overview
The crystal structure of the replication terminator protein (RTP) of B. subtilis has been determined at 2.6 A resolution. As previously suggested by both biochemical and biophysical studies, the molecule exists as a symmetric dimer and is in the alpha + beta protein-folding class. The protein has several uncommon features, including an antiparallel coiled-coil, which serves as the dimerization domain, and both an alpha-helix and a beta-ribbon suitably positioned to interact with the major and minor grooves of B-DNA. A site has been identified on the surface of RTP that is biochemically and positionally suitable for interaction with the replication-specific helicase. Other features of the structure are consistent with the polar contrahelicase mechanism of the protein. A model of the interaction between RTP and its cognate DNA is presented.
About this Structure
1BM9 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Crystal structure of the replication terminator protein from B. subtilis at 2.6 A., Bussiere DE, Bastia D, White SW, Cell. 1995 Feb 24;80(4):651-60. PMID:7867072
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