1fs0
From Proteopedia
(New page: 200px<br /><applet load="1fs0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fs0, resolution 2.1Å" /> '''COMPLEX OF GAMMA/EPSI...) |
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| - | [[Image:1fs0.jpg|left|200px]]<br /><applet load="1fs0" size=" | + | [[Image:1fs0.jpg|left|200px]]<br /><applet load="1fs0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fs0, resolution 2.1Å" /> | caption="1fs0, resolution 2.1Å" /> | ||
'''COMPLEX OF GAMMA/EPSILON ATP SYNTHASE FROM E.COLI'''<br /> | '''COMPLEX OF GAMMA/EPSILON ATP SYNTHASE FROM E.COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | ATP synthases (F(1)F(o)-ATPases) use energy released by the movement of | + | ATP synthases (F(1)F(o)-ATPases) use energy released by the movement of protons down a transmembrane electrochemical gradient to drive the synthesis of ATP, the universal biological energy currency. Proton flow through F(o) drives rotation of a ring of c-subunits and a complex of the gamma and epsilon-subunits, causing cyclical conformational changes in F(1) that are required for catalysis. The crystal structure of a large portion of F(1) has been resolved. However, the structure of the central portion of the enzyme, through which conformational changes in F(o) are communicated to F(1), has until now remained elusive. Here we report the crystal structure of a complex of the epsilon-subunit and the central domain of the gamma-subunit refined at 2.1 A resolution. The structure reveals how rotation of these subunits causes large conformational changes in F(1), and thereby provides new insights into energy coupling between F(o) and F(1). |
==About this Structure== | ==About this Structure== | ||
| - | 1FS0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] Full crystallographic information is available from [http:// | + | 1FS0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FS0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: H(+)-transporting two-sector ATPase]] | [[Category: H(+)-transporting two-sector ATPase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Rodgers, A | + | [[Category: Rodgers, A J.W.]] |
| - | [[Category: Wilce, M | + | [[Category: Wilce, M C.J.]] |
[[Category: atp synthase]] | [[Category: atp synthase]] | ||
[[Category: coiled coil]] | [[Category: coiled coil]] | ||
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[[Category: gamma]] | [[Category: gamma]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:41:59 2008'' |
Revision as of 10:42, 21 February 2008
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COMPLEX OF GAMMA/EPSILON ATP SYNTHASE FROM E.COLI
Overview
ATP synthases (F(1)F(o)-ATPases) use energy released by the movement of protons down a transmembrane electrochemical gradient to drive the synthesis of ATP, the universal biological energy currency. Proton flow through F(o) drives rotation of a ring of c-subunits and a complex of the gamma and epsilon-subunits, causing cyclical conformational changes in F(1) that are required for catalysis. The crystal structure of a large portion of F(1) has been resolved. However, the structure of the central portion of the enzyme, through which conformational changes in F(o) are communicated to F(1), has until now remained elusive. Here we report the crystal structure of a complex of the epsilon-subunit and the central domain of the gamma-subunit refined at 2.1 A resolution. The structure reveals how rotation of these subunits causes large conformational changes in F(1), and thereby provides new insights into energy coupling between F(o) and F(1).
About this Structure
1FS0 is a Protein complex structure of sequences from Escherichia coli. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Full crystallographic information is available from OCA.
Reference
Structure of the gamma-epsilon complex of ATP synthase., Rodgers AJ, Wilce MC, Nat Struct Biol. 2000 Nov;7(11):1051-4. PMID:11062562
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