2bl2
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The membrane rotor ring from the vacuolar-type (V-type) sodium ion-pumping | + | The membrane rotor ring from the vacuolar-type (V-type) sodium ion-pumping adenosine triphosphatase (Na+-ATPase) from Enterococcus hirae consists of 10 NtpK subunits, which are homologs of the 16-kilodalton and 8-kilodalton proteolipids found in other V-ATPases and in F1Fo- or F-ATPases, respectively. Each NtpK subunit has four transmembrane alpha helices, with a sodium ion bound between helices 2 and 4 at a site buried deeply in the membrane that includes the essential residue glutamate-139. This site is probably connected to the membrane surface by two half-channels in subunit NtpI, against which the ring rotates. Symmetry mismatch between the rotor and catalytic domains appears to be an intrinsic feature of both V- and F-ATPases. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Kakinuma, Y.]] | [[Category: Kakinuma, Y.]] | ||
| - | [[Category: Leslie, A | + | [[Category: Leslie, A G.W.]] |
[[Category: Murata, T.]] | [[Category: Murata, T.]] | ||
| - | [[Category: Walker, J | + | [[Category: Walker, J E.]] |
[[Category: Yamato, I.]] | [[Category: Yamato, I.]] | ||
[[Category: LHG]] | [[Category: LHG]] | ||
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[[Category: v-type atpase]] | [[Category: v-type atpase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:38:55 2008'' |
Revision as of 14:38, 21 February 2008
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THE MEMBRANE ROTOR OF THE V-TYPE ATPASE FROM ENTEROCOCCUS HIRAE
Overview
The membrane rotor ring from the vacuolar-type (V-type) sodium ion-pumping adenosine triphosphatase (Na+-ATPase) from Enterococcus hirae consists of 10 NtpK subunits, which are homologs of the 16-kilodalton and 8-kilodalton proteolipids found in other V-ATPases and in F1Fo- or F-ATPases, respectively. Each NtpK subunit has four transmembrane alpha helices, with a sodium ion bound between helices 2 and 4 at a site buried deeply in the membrane that includes the essential residue glutamate-139. This site is probably connected to the membrane surface by two half-channels in subunit NtpI, against which the ring rotates. Symmetry mismatch between the rotor and catalytic domains appears to be an intrinsic feature of both V- and F-ATPases.
About this Structure
2BL2 is a Single protein structure of sequence from Enterococcus hirae with , and as ligands. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae., Murata T, Yamato I, Kakinuma Y, Leslie AG, Walker JE, Science. 2005 Apr 29;308(5722):654-9. Epub 2005 Mar 31. PMID:15802565
Page seeded by OCA on Thu Feb 21 16:38:55 2008
