1m74: Difference between revisions

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[[Image:1m74.~~gif~~|left|200px]]

[[Image:1m74.png|left|200px]]

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~~'''~~Crystal structure of Mg-ADP-bound SecA from Bacillus subtilis~~'''~~

===Crystal structure of Mg-ADP-bound SecA from Bacillus subtilis===

~~==Overview==~~

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The ~~SecA adenosine triphosphatase (ATPase) mediates extrusion of~~ the ~~amino termini of secreted proteins from~~ the ~~eubacterial cytosol based~~ on ~~cycles of reversible binding to the SecYEG translocon. We have determined the crystal structure of SecA with and without magnesium-adenosine diphosphate bound to the high-affinity ATPase site~~ at 3.~~0 and 2~~.~~7 angstrom resolution~~, ~~respectively. Candidate sites for preprotein binding are located on a surface containing~~ the ~~SecA epitopes exposed to the periplasm upon binding to SecYEG and are thus positioned to deliver preprotein to SecYEG~~. ~~Comparisons with structurally related ATPases, including superfamily I and II ATP~~-dependent helicases, suggest that the interaction geometry of the tandem motor domains in SecA is modulated by nucleotide binding, which is shown by fluorescence anisotropy experiments to reverse an endothermic domain-~~dissociation reaction hypothesized to gate binding to SecYEG.~~

The line below this paragraph, {{ABSTRACT_PUBMED_12242434}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12242434 is the PubMed ID number.

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==About this Structure==

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[[Category: Protein translocation]]

[[Category: Transmembrane transport]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May~~ ~~3 00~~:43:04 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:21:32 2008''

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-[[Image:1m74.gif|left|200px]]
+{{Seed}}
+[[Image:1m74.png|left|200px]]
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 {{STRUCTURE_1m74|  PDB=1m74  |  SCENE=  }}
-'''Crystal structure of Mg-ADP-bound SecA from Bacillus subtilis'''
+===Crystal structure of Mg-ADP-bound SecA from Bacillus subtilis===
-==Overview==
+<!--
-The SecA adenosine triphosphatase (ATPase) mediates extrusion of the amino termini of secreted proteins from the eubacterial cytosol based on cycles of reversible binding to the SecYEG translocon. We have determined the crystal structure of SecA with and without magnesium-adenosine diphosphate bound to the high-affinity ATPase site at 3.0 and 2.7 angstrom resolution, respectively. Candidate sites for preprotein binding are located on a surface containing the SecA epitopes exposed to the periplasm upon binding to SecYEG and are thus positioned to deliver preprotein to SecYEG. Comparisons with structurally related ATPases, including superfamily I and II ATP-dependent helicases, suggest that the interaction geometry of the tandem motor domains in SecA is modulated by nucleotide binding, which is shown by fluorescence anisotropy experiments to reverse an endothermic domain-dissociation reaction hypothesized to gate binding to SecYEG.
+The line below this paragraph, {{ABSTRACT_PUBMED_12242434}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12242434 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12242434}}
 ==About this Structure==
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 [[Category: Protein translocation]]
 [[Category: Transmembrane transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:43:04 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 23:21:32 2008''