2bl2

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Image:2bl2.gif

2bl2, resolution 2.10Å

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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

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