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1ixz

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(New page: 200px<br /><applet load="1ixz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ixz, resolution 2.2&Aring;" /> '''Crystal structure of ...)
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[[Image:1ixz.gif|left|200px]]<br /><applet load="1ixz" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1ixz, resolution 2.2&Aring;" />
'''Crystal structure of the FtsH ATPase domain from Thermus thermophilus'''<br />
'''Crystal structure of the FtsH ATPase domain from Thermus thermophilus'''<br />
==Overview==
==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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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.
==About this Structure==
==About this Structure==
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1IXZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with HG and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IXZ OCA].
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1IXZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=HG:'>HG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IXZ OCA].
==Reference==
==Reference==
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[[Category: aaa domain fold]]
[[Category: aaa domain fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:45:08 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:16:52 2008''

Revision as of 11:16, 21 February 2008


1ixz, resolution 2.2Å

Drag the structure with the mouse to rotate

Crystal structure of the FtsH ATPase domain from Thermus thermophilus

Overview

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.

About this Structure

1IXZ is a Single protein structure of sequence from Thermus thermophilus with and as ligands. Full crystallographic information is available from OCA.

Reference

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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