1z47
From Proteopedia
(New page: 200px<br /><applet load="1z47" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z47, resolution 1.90Å" /> '''Structure of the ATP...) |
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| - | [[Image:1z47.gif|left|200px]]<br /><applet load="1z47" size=" | + | [[Image:1z47.gif|left|200px]]<br /><applet load="1z47" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1z47, resolution 1.90Å" /> | caption="1z47, resolution 1.90Å" /> | ||
'''Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius'''<br /> | '''Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius'''<br /> | ||
==Overview== | ==Overview== | ||
| - | CysA, the ATPase subunit of a putative sulfate ATP-binding cassette | + | CysA, the ATPase subunit of a putative sulfate ATP-binding cassette transport system of the gram-positive thermoacidophilic bacterium Alicyclobacillus acidocaldarius, was structurally characterized at a resolution of 2.0 Angstroms in the absence of nucleotides. In line with previous findings on ABC-ATPases the structures of the two monomers (called CysA-1 and CysA-2) in the asymmetric unit differ substantially in the arrangement of their individual (sub)domains. CysA-2 was found as a physiological dimer composed of two crystallographically related monomers that are arranged in an open state. Interestingly, while the regulatory domain of CysA-2 packs against its opposing domain that of CysA-1 undergoes a conformational change and, in the dimer, would interfere with the opposing monomer thereby preventing solute translocation. Whether this conformational state is used for regulatory purposes will be discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1Z47 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius Alicyclobacillus acidocaldarius] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1Z47 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius Alicyclobacillus acidocaldarius] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z47 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: alpha/beta motif; beta sandwich]] | [[Category: alpha/beta motif; beta sandwich]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:11:56 2008'' |
Revision as of 14:11, 21 February 2008
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Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius
Overview
CysA, the ATPase subunit of a putative sulfate ATP-binding cassette transport system of the gram-positive thermoacidophilic bacterium Alicyclobacillus acidocaldarius, was structurally characterized at a resolution of 2.0 Angstroms in the absence of nucleotides. In line with previous findings on ABC-ATPases the structures of the two monomers (called CysA-1 and CysA-2) in the asymmetric unit differ substantially in the arrangement of their individual (sub)domains. CysA-2 was found as a physiological dimer composed of two crystallographically related monomers that are arranged in an open state. Interestingly, while the regulatory domain of CysA-2 packs against its opposing domain that of CysA-1 undergoes a conformational change and, in the dimer, would interfere with the opposing monomer thereby preventing solute translocation. Whether this conformational state is used for regulatory purposes will be discussed.
About this Structure
1Z47 is a Single protein structure of sequence from Alicyclobacillus acidocaldarius with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius., Scheffel F, Demmer U, Warkentin E, Hulsmann A, Schneider E, Ermler U, FEBS Lett. 2005 May 23;579(13):2953-8. Epub 2005 Apr 25. PMID:15893314
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