1iy1: Difference between revisions

New page: left|200px<br /><applet load="1iy1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iy1, resolution 2.8Å" /> '''Crystal structure of ...
 
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[[Image:1iy1.jpg|left|200px]]<br /><applet load="1iy1" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1iy1.jpg|left|200px]]<br /><applet load="1iy1" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1iy1, resolution 2.8&Aring;" />
caption="1iy1, resolution 2.8&Aring;" />
'''Crystal structure of the FtsH ATPase domain with ADP from Thermus thermophilus'''<br />
'''Crystal structure of the FtsH ATPase domain with ADP from Thermus thermophilus'''<br />


==Overview==
==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.
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==
1IY1 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 ADP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IY1 OCA].  
1IY1 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=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IY1 OCA].  


==Reference==
==Reference==
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[[Category: aaa domain fold]]
[[Category: aaa domain fold]]


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