1twb: Difference between revisions

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

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

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~~'''~~SspB disulfide crosslinked to an ssrA degradation tag~~'''~~

===SspB disulfide crosslinked to an ssrA degradation tag===

~~==Overview==~~

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The ~~SspB adaptor enhances ClpXP degradation by binding the ssrA degradation tag of substrates and the AAA+ ClpX unfoldase. To probe the mechanism of substrate delivery~~, we engineered a disulfide bond between the ssrA tag and SspB and demonstrated otherwise normal interactions by solving the crystal structure. Although the covalent link prevents adaptor.substrate dissociation, ~~ClpXP degraded GFP-ssrA that was disulfide bonded to~~ the ~~adaptor. Thus, crosslinked substrate must be handed directly from SspB~~ to ~~ClpX. The ssrA tag in~~ the ~~covalent adaptor complex interacted with ClpX~~.~~ATPgammaS but not ClpX~~.~~ADP~~, ~~suggesting that handoff occurs in~~ the ATP bound enzyme. By contrast, SspB alone bound ClpX in both nucleotide states. Similar handoff mechanisms will undoubtedly be used by many AAA+ adaptors and enzymes, allowing assembly of delivery complexes in either nucleotide state, engagement of the recognition tag in the ATP state, and application of an unfolding force to the attached protein following hydrolysis.

The line below this paragraph, {{ABSTRACT_PUBMED_15525508}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15525508 is the PubMed ID number.

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==About this Structure==

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[[Category: Protease]]

[[Category: Specificity factor]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 10~~:27:01 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:24:26 2008''

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-[[Image:1twb.gif|left|200px]]
+{{Seed}}
+[[Image:1twb.png|left|200px]]
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 {{STRUCTURE_1twb|  PDB=1twb  |  SCENE=  }}
-'''SspB disulfide crosslinked to an ssrA degradation tag'''
+===SspB disulfide crosslinked to an ssrA degradation tag===
-==Overview==
+<!--
-The SspB adaptor enhances ClpXP degradation by binding the ssrA degradation tag of substrates and the AAA+ ClpX unfoldase. To probe the mechanism of substrate delivery, we engineered a disulfide bond between the ssrA tag and SspB and demonstrated otherwise normal interactions by solving the crystal structure. Although the covalent link prevents adaptor.substrate dissociation, ClpXP degraded GFP-ssrA that was disulfide bonded to the adaptor. Thus, crosslinked substrate must be handed directly from SspB to ClpX. The ssrA tag in the covalent adaptor complex interacted with ClpX.ATPgammaS but not ClpX.ADP, suggesting that handoff occurs in the ATP bound enzyme. By contrast, SspB alone bound ClpX in both nucleotide states. Similar handoff mechanisms will undoubtedly be used by many AAA+ adaptors and enzymes, allowing assembly of delivery complexes in either nucleotide state, engagement of the recognition tag in the ATP state, and application of an unfolding force to the attached protein following hydrolysis.
+The line below this paragraph, {{ABSTRACT_PUBMED_15525508}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15525508 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15525508}}
 ==About this Structure==
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 [[Category: Protease]]
 [[Category: Specificity factor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:27:01 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:24:26 2008''