1tf2
From Proteopedia
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|PDB= 1tf2 |SIZE=350|CAPTION= <scene name='initialview01'>1tf2</scene>, resolution 2.90Å | |PDB= 1tf2 |SIZE=350|CAPTION= <scene name='initialview01'>1tf2</scene>, resolution 2.90Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= SECA, DIV+, BSU35300 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | |GENE= SECA, DIV+, BSU35300 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1tf5|1TF5]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tf2 OCA], [http://www.ebi.ac.uk/pdbsum/1tf2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tf2 RCSB]</span> | ||
}} | }} | ||
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[[Category: Osborne, A R.]] | [[Category: Osborne, A R.]] | ||
[[Category: Rapoport, T A.]] | [[Category: Rapoport, T A.]] | ||
- | [[Category: ADP]] | ||
- | [[Category: MG]] | ||
[[Category: atpase]] | [[Category: atpase]] | ||
[[Category: helicase]] | [[Category: helicase]] | ||
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[[Category: translocation]] | [[Category: translocation]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:55:10 2008'' |
Revision as of 20:55, 30 March 2008
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, resolution 2.90Å | |||||||
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Ligands: | , | ||||||
Gene: | SECA, DIV+, BSU35300 (Bacillus subtilis) | ||||||
Related: | 1TF5
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of SecA:ADP in an open conformation from Bacillus Subtilis
Overview
The ATPase SecA mediates the posttranslational translocation of a wide range of polypeptide substrates through the SecY channel in the cytoplasmic membrane of bacteria. We have determined the crystal structure of a monomeric form of Bacillus subtilis SecA at a 2.2-A resolution. A comparison with the previously determined structures of SecA reveals a nucleotide-independent, large conformational change that opens a deep groove similar to that in other proteins that interact with diverse polypeptides. We propose that the open form of SecA represents an activated state.
About this Structure
1TF2 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
A large conformational change of the translocation ATPase SecA., Osborne AR, Clemons WM Jr, Rapoport TA, Proc Natl Acad Sci U S A. 2004 Jul 27;101(30):10937-42. Epub 2004 Jul 15. PMID:15256599
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