2di4: Difference between revisions

Revision as of 20:01, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2di4.png

Template:STRUCTURE 2di4

Crystal structure of the FtsH protease domainCrystal structure of the FtsH protease domain

Template:ABSTRACT PUBMED 16762831

About this StructureAbout this Structure

2DI4 is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the whole cytosolic region of ATP-dependent protease FtsH., Suno R, Niwa H, Tsuchiya D, Zhang X, Yoshida M, Morikawa K, Mol Cell. 2006 Jun 9;22(5):575-85. PMID:16762831

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

Page seeded by OCA on Sun Jul 27 20:01:10 2008

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OCA

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-[[Image:2di4.gif|left|200px]]
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 {{STRUCTURE_2di4|  PDB=2di4  |  SCENE=  }}
-'''Crystal structure of the FtsH protease domain'''
+===Crystal structure of the FtsH protease domain===
-==Overview==
+<!--
-An ATP-dependent protease, FtsH, digests misassembled membrane proteins in order to maintain membrane integrity and digests short-lived soluble proteins in order to control their cellular regulation. This enzyme has an N-terminal transmembrane segment and a C-terminal cytosolic region consisting of an AAA+ ATPase domain and a protease domain. Here we present two crystal structures: the protease domain and the whole cytosolic region. The cytosolic region fully retains an ATP-dependent protease activity and adopts a three-fold-symmetric hexameric structure. The protease domains displayed a six-fold symmetry, while the AAA+ domains, each containing ADP, alternate two orientations relative to the protease domain, making "open" and "closed" interdomain contacts. Apparently, ATPase is active only in the closed form, and protease operates in the open form. The protease catalytic sites are accessible only through a tunnel following from the AAA+ domain of the adjacent subunit, raising a possibility of translocation of polypeptide substrate to the protease sites through this tunnel.
+The line below this paragraph, {{ABSTRACT_PUBMED_16762831}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16762831 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16762831}}
 ==About this Structure==
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 ==Reference==
 Structure of the whole cytosolic region of ATP-dependent protease FtsH., Suno R, Niwa H, Tsuchiya D, Zhang X, Yoshida M, Morikawa K, Mol Cell. 2006 Jun 9;22(5):575-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16762831 16762831]
+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:[http://www.ncbi.nlm.nih.gov/pubmed/12377127 12377127]
 [[Category: Aquifex aeolicus]]
 [[Category: Single protein]]
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 [[Category: Hexamer-ring]]
 [[Category: Metalloproteinase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 00:28:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:01:10 2008''