2fxt: Difference between revisions

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~~'''~~Crystal Structure of Yeast Tim44~~'''~~

===Crystal Structure of Yeast Tim44===

~~==Overview==~~

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The ~~protein transports from~~ the ~~cell cytosol~~ to the ~~mitochondria matrix are carried out by the translocase of the outer membrane~~ (~~TOM) complex and the translocase of the inner membrane (TIM) complexes~~. ~~Tim44p is an essential mitochondrial peripheral membrane protein and a major component of TIM23 translocon~~. ~~Tim44p can tightly associate with the inner mitochondrial membrane. To investigate the mechanism by which Tim44p functions in the TIM23 translocon to deliver the mitochondrial protein precursors~~, ~~we have determined~~ the ~~crystal structure of the yeast Tim44p C-terminal domain to 3~~.~~2A resolution using the MAD method. The Tim44p C~~-~~terminal domain forms a monomer in the crystal structure and contains six alpha~~-helices and four antiparallel beta-strands. A large hydrophobic pocket was identified on the Tim44p structure surface. The N-terminal helix A1 is positively charged and the helix A1 protrudes out from the Tim44p main body.

The line below this paragraph, {{ABSTRACT_PUBMED_16647716}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16647716 is the PubMed ID number.

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==About this Structure==

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[[Category: Sha, B.]]

[[Category: Mitochondrial translocase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 04~~:25:47 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:59:50 2008''

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-[[Image:2fxt.jpg|left|200px]]
+{{Seed}}
+[[Image:2fxt.png|left|200px]]
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 {{STRUCTURE_2fxt|  PDB=2fxt  |  SCENE=  }}
-'''Crystal Structure of Yeast Tim44'''
+===Crystal Structure of Yeast Tim44===
-==Overview==
+<!--
-The protein transports from the cell cytosol to the mitochondria matrix are carried out by the translocase of the outer membrane (TOM) complex and the translocase of the inner membrane (TIM) complexes. Tim44p is an essential mitochondrial peripheral membrane protein and a major component of TIM23 translocon. Tim44p can tightly associate with the inner mitochondrial membrane. To investigate the mechanism by which Tim44p functions in the TIM23 translocon to deliver the mitochondrial protein precursors, we have determined the crystal structure of the yeast Tim44p C-terminal domain to 3.2A resolution using the MAD method. The Tim44p C-terminal domain forms a monomer in the crystal structure and contains six alpha-helices and four antiparallel beta-strands. A large hydrophobic pocket was identified on the Tim44p structure surface. The N-terminal helix A1 is positively charged and the helix A1 protrudes out from the Tim44p main body.
+The line below this paragraph, {{ABSTRACT_PUBMED_16647716}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16647716 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16647716}}
 ==About this Structure==
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 [[Category: Sha, B.]]
 [[Category: Mitochondrial translocase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 04:25:47 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:59:50 2008''