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1nbw

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{{STRUCTURE_1nbw| PDB=1nbw | SCENE= }}
{{STRUCTURE_1nbw| PDB=1nbw | SCENE= }}
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'''Glycerol dehydratase reactivase'''
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===Glycerol dehydratase reactivase===
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==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.
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==About this Structure==
==About this Structure==
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[[Category: Molecular chaperone]]
[[Category: Molecular chaperone]]
[[Category: Reactivase]]
[[Category: Reactivase]]
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Revision as of 14:30, 27 July 2008

Image:1nbw.png

Template:STRUCTURE 1nbw

Glycerol dehydratase reactivase

Template:ABSTRACT PUBMED 12517345

About this Structure

1NBW is a Protein complex structure of sequences from Klebsiella pneumoniae. Full crystallographic information is available from OCA.

Reference

Structure of glycerol dehydratase reactivase: a new type of molecular chaperone., Liao DI, Reiss L, Turner I, Dotson G, Structure. 2003 Jan;11(1):109-19. PMID:12517345

Page seeded by OCA on Sun Jul 27 17:29:51 2008

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