2bl2
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(New page: 200px<br /> <applet load="2bl2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bl2, resolution 2.10Å" /> '''THE MEMBRANE ROTOR ...)
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Revision as of 19:06, 29 October 2007
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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 NA, LHG and UMQ as [ligands]. Active as [[1]], with EC number [3.6.3.14]. 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 Mon Oct 29 21:11:35 2007
