1m74
From Proteopedia
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|PDB= 1m74 |SIZE=350|CAPTION= <scene name='initialview01'>1m74</scene>, resolution 3.00Å | |PDB= 1m74 |SIZE=350|CAPTION= <scene name='initialview01'>1m74</scene>, resolution 3.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= Div ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | |GENE= Div ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1m6n|1M6N]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m74 OCA], [http://www.ebi.ac.uk/pdbsum/1m74 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m74 RCSB]</span> | ||
}} | }} | ||
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[[Category: Oliver, D B.]] | [[Category: Oliver, D B.]] | ||
[[Category: Weinkauf, S.]] | [[Category: Weinkauf, S.]] | ||
| - | [[Category: | + | [[Category: atpase]] |
| - | [[Category: | + | [[Category: helicase family structure]] |
| - | [[Category: | + | [[Category: mechanochemisty]] |
| - | [[Category: protein translocation | + | [[Category: protein translocation]] |
| + | [[Category: transmembrane transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:12:14 2008'' |
Revision as of 19:12, 30 March 2008
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| , resolution 3.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | Div (Bacillus subtilis) | ||||||
| Related: | 1M6N
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
1M74 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA., Hunt JF, Weinkauf S, Henry L, Fak JJ, McNicholas P, Oliver DB, Deisenhofer J, Science. 2002 Sep 20;297(5589):2018-26. PMID:12242434
Page seeded by OCA on Sun Mar 30 22:12:14 2008
