1f48
From Proteopedia
(New page: 200px<br /><applet load="1f48" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f48, resolution 2.30Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1f48.jpg|left|200px]]<br /><applet load="1f48" size=" | + | [[Image:1f48.jpg|left|200px]]<br /><applet load="1f48" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1f48, resolution 2.30Å" /> | caption="1f48, resolution 2.30Å" /> | ||
'''CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ATPASE'''<br /> | '''CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ATPASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Active extrusion is a common mechanism underlying detoxification of heavy | + | Active extrusion is a common mechanism underlying detoxification of heavy metals, drugs and antibiotics in bacteria, protozoa and mammals. In Escherichia coli, the ArsAB pump provides resistance to arsenite and antimonite. This pump consists of a soluble ATPase (ArsA) and a membrane channel (ArsB). ArsA contains two nucleotide-binding sites (NBSs) and a binding site for arsenic or antimony. Binding of metalloids stimulates ATPase activity. The crystal structure of ArsA reveals that both NBSs and the metal-binding site are located at the interface between two homologous domains. A short stretch of residues connecting the metal-binding site to the NBSs provides a signal transduction pathway that conveys information on metal occupancy to the ATP hydrolysis sites. Based on these structural features, we propose that the metal-binding site is involved directly in the process of vectorial translocation of arsenite or antimonite across the membrane. The relative positions of the NBS and the inferred mechanism of allosteric activation of ArsA provide a useful model for the interaction of the catalytic domains in other transport ATPases. |
==About this Structure== | ==About this Structure== | ||
| - | 1F48 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SB, MG, CD, CL, SBO and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1F48 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SB:'>SB</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CD:'>CD</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=SBO:'>SBO</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F48 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Gatti, D | + | [[Category: Gatti, D L.]] |
[[Category: Radaev, S.]] | [[Category: Radaev, S.]] | ||
| - | [[Category: Rosen, B | + | [[Category: Rosen, B P.]] |
[[Category: Zhou, T.]] | [[Category: Zhou, T.]] | ||
[[Category: ADP]] | [[Category: ADP]] | ||
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[[Category: p-loop]] | [[Category: p-loop]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:40 2008'' |
Revision as of 10:34, 21 February 2008
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CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ATPASE
Overview
Active extrusion is a common mechanism underlying detoxification of heavy metals, drugs and antibiotics in bacteria, protozoa and mammals. In Escherichia coli, the ArsAB pump provides resistance to arsenite and antimonite. This pump consists of a soluble ATPase (ArsA) and a membrane channel (ArsB). ArsA contains two nucleotide-binding sites (NBSs) and a binding site for arsenic or antimony. Binding of metalloids stimulates ATPase activity. The crystal structure of ArsA reveals that both NBSs and the metal-binding site are located at the interface between two homologous domains. A short stretch of residues connecting the metal-binding site to the NBSs provides a signal transduction pathway that conveys information on metal occupancy to the ATP hydrolysis sites. Based on these structural features, we propose that the metal-binding site is involved directly in the process of vectorial translocation of arsenite or antimonite across the membrane. The relative positions of the NBS and the inferred mechanism of allosteric activation of ArsA provide a useful model for the interaction of the catalytic domains in other transport ATPases.
About this Structure
1F48 is a Single protein structure of sequence from Escherichia coli with , , , , and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump., Zhou T, Radaev S, Rosen BP, Gatti DL, EMBO J. 2000 Sep 1;19(17):4838-45. PMID:10970874
Page seeded by OCA on Thu Feb 21 12:34:40 2008
Categories: Escherichia coli | Single protein | Gatti, D L. | Radaev, S. | Rosen, B P. | Zhou, T. | ADP | CD | CL | MG | SB | SBO | Antimonite binding site | Atp binding site | P-loop
