1hqc: Difference between revisions

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[[Image:1hqc.~~gif~~|left|200px]]

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

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~~'''~~STRUCTURE OF RUVB FROM THERMUS THERMOPHILUS HB8~~'''~~

===STRUCTURE OF RUVB FROM THERMUS THERMOPHILUS HB8===

~~==Overview==~~

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~~We report here the crystal structure of the RuvB motor protein from Thermus thermophilus HB8~~, ~~which drives branch migration of the Holliday junction during homologous recombination. RuvB has a crescent-like architecture consisting of three consecutive domains~~, the ~~first two of which are involved in ATP binding and hydrolysis. DNA is likely~~ to ~~interact with a large basic cleft, which encompasses~~ the ~~ATP-binding pocket and domain boundaries~~, ~~whereas~~ the ~~junction-recognition protein RuvA may bind a flexible beta-hairpin protruding from the N-terminal domain~~. ~~The structures of two subunits, related by a noncrystallographic pseudo~~-2-~~fold axis, imply that conformational changes of motor protein coupled with ATP hydrolysis may reflect motility essential for its translocation around double-stranded DNA.~~

The line below this paragraph, {{ABSTRACT_PUBMED_11171970}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11171970 is the PubMed ID number.

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==About this Structure==

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[[Category: Extended aaa-atpase domain]]

[[Category: Ruvb]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 19~~:07:15 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:32:15 2008''

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-[[Image:1hqc.gif|left|200px]]
+{{Seed}}
+[[Image:1hqc.png|left|200px]]
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 {{STRUCTURE_1hqc|  PDB=1hqc  |  SCENE=  }}
-'''STRUCTURE OF RUVB FROM THERMUS THERMOPHILUS HB8'''
+===STRUCTURE OF RUVB FROM THERMUS THERMOPHILUS HB8===
-==Overview==
+<!--
-We report here the crystal structure of the RuvB motor protein from Thermus thermophilus HB8, which drives branch migration of the Holliday junction during homologous recombination. RuvB has a crescent-like architecture consisting of three consecutive domains, the first two of which are involved in ATP binding and hydrolysis. DNA is likely to interact with a large basic cleft, which encompasses the ATP-binding pocket and domain boundaries, whereas the junction-recognition protein RuvA may bind a flexible beta-hairpin protruding from the N-terminal domain. The structures of two subunits, related by a noncrystallographic pseudo-2-fold axis, imply that conformational changes of motor protein coupled with ATP hydrolysis may reflect motility essential for its translocation around double-stranded DNA.
+The line below this paragraph, {{ABSTRACT_PUBMED_11171970}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11171970 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11171970}}
 ==About this Structure==
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 [[Category: Extended aaa-atpase domain]]
 [[Category: Ruvb]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:07:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 08:32:15 2008''