1nbw: Difference between revisions

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

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

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~~'''~~Glycerol dehydratase reactivase~~'''~~

===Glycerol dehydratase reactivase===

~~==Overview==~~

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The ~~function of glycerol dehydratase (GDH) reactivase is~~ to ~~remove damaged coenzyme B~~(~~12) from GDH that has suffered mechanism-based inactivation. The structure of GDH reactivase from Klebsiella pneumoniae was determined~~ at ~~2.4 A resolution by the single isomorphous replacement with anomalous signal (SIR~~/~~AS) method~~. ~~Each tetramer contains two elongated 63 kDa alpha subunits and two globular 14 kDa beta subunits~~. ~~The alpha subunit contains structural features resembling both GroEL and Hsp70 groups of chaperones~~, ~~and it appears chaperone like in its interactions with ATP. The fold of~~ the beta subunit resembles that of the beta subunit of glycerol dehydratase, except that it lacks some coenzyme B(12) binding elements. A hypothesis for the reactivation mechanism of reactivase is proposed based on these structural features.

The line below this paragraph, {{ABSTRACT_PUBMED_12517345}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12517345 is the PubMed ID number.

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==About this Structure==

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[[Category: Molecular chaperone]]

[[Category: Reactivase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 02~~:20:45 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:29:51 2008''

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-[[Image:1nbw.jpg|left|200px]]
+{{Seed}}
+[[Image:1nbw.png|left|200px]]
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 {{STRUCTURE_1nbw|  PDB=1nbw  |  SCENE=  }}
-'''Glycerol dehydratase reactivase'''
+===Glycerol dehydratase reactivase===
-==Overview==
+<!--
-The function of glycerol dehydratase (GDH) reactivase is to remove damaged coenzyme B(12) from GDH that has suffered mechanism-based inactivation. The structure of GDH reactivase from Klebsiella pneumoniae was determined at 2.4 A resolution by the single isomorphous replacement with anomalous signal (SIR/AS) method. Each tetramer contains two elongated 63 kDa alpha subunits and two globular 14 kDa beta subunits. The alpha subunit contains structural features resembling both GroEL and Hsp70 groups of chaperones, and it appears chaperone like in its interactions with ATP. The fold of the beta subunit resembles that of the beta subunit of glycerol dehydratase, except that it lacks some coenzyme B(12) binding elements. A hypothesis for the reactivation mechanism of reactivase is proposed based on these structural features.
+The line below this paragraph, {{ABSTRACT_PUBMED_12517345}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12517345 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12517345}}
 ==About this Structure==
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 [[Category: Molecular chaperone]]
 [[Category: Reactivase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:20:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:29:51 2008''