1bm9: Difference between revisions

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[[Image:1bm9.~~jpg~~|left|200px]]

[[Image:1bm9.png|left|200px]]

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~~'''~~REPLICATION TERMINATOR PROTEIN FROM BACILLUS SUBTILIS~~'''~~

===REPLICATION TERMINATOR PROTEIN FROM BACILLUS SUBTILIS===

~~==Overview==~~

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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.

The line below this paragraph, {{ABSTRACT_PUBMED_7867072}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 7867072 is the PubMed ID number.

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==About this Structure==

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[[Category: Contrahelicase]]

[[Category: Dna-binding protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 11~~:41~~:34~~ 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:22:41 2008''

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-[[Image:1bm9.jpg|left|200px]]
+{{Seed}}
+[[Image:1bm9.png|left|200px]]
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 {{STRUCTURE_1bm9|  PDB=1bm9  |  SCENE=  }}
-'''REPLICATION TERMINATOR PROTEIN FROM BACILLUS SUBTILIS'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_7867072}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7867072 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7867072}}
 ==About this Structure==
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 [[Category: Contrahelicase]]
 [[Category: Dna-binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:41:34 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:22:41 2008''