1iy0: Difference between revisions

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{{STRUCTURE_1iy0|  PDB=1iy0  |  SCENE=  }}  
{{STRUCTURE_1iy0|  PDB=1iy0  |  SCENE=  }}  


'''Crystal structure of the FtsH ATPase domain with AMP-PNP from Thermus thermophilus'''
===Crystal structure of the FtsH ATPase domain with AMP-PNP from Thermus thermophilus===




==Overview==
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FtsH is a cytoplasmic membrane-integrated, ATP-dependent metalloprotease, which processively degrades both cytoplasmic and membrane proteins in concert with unfolding. The FtsH protein is divided into the N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. We have determined the crystal structures of the Thermus thermophilus FtsH ATPase domain in the nucleotide-free and AMP-PNP- and ADP-bound states, in addition to the domain with the extra preceding segment. Combined with the mapping of the putative substrate binding region, these structures suggest that FtsH internally forms a hexameric ring structure, in which ATP binding could cause a conformational change to facilitate transport of substrates into the protease domain through the central pore.
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{{ABSTRACT_PUBMED_12377127}}


==About this Structure==
==About this Structure==
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[[Category: Yoshida, M.]]
[[Category: Yoshida, M.]]
[[Category: Aaa domain fold]]
[[Category: Aaa domain fold]]
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Revision as of 14:11, 1 July 2008

File:1iy0.png

Template:STRUCTURE 1iy0

Crystal structure of the FtsH ATPase domain with AMP-PNP from Thermus thermophilusCrystal structure of the FtsH ATPase domain with AMP-PNP from Thermus thermophilus

Template:ABSTRACT PUBMED 12377127

About this StructureAbout this Structure

1IY0 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

ReferenceReference

Hexameric ring structure of the ATPase domain of the membrane-integrated metalloprotease FtsH from Thermus thermophilus HB8., Niwa H, Tsuchiya D, Makyio H, Yoshida M, Morikawa K, Structure. 2002 Oct;10(10):1415-23. PMID:12377127

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