2bl2: Difference between revisions
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|PDB= 2bl2 |SIZE=350|CAPTION= <scene name='initialview01'>2bl2</scene>, resolution 2.10Å | |PDB= 2bl2 |SIZE=350|CAPTION= <scene name='initialview01'>2bl2</scene>, resolution 2.10Å | ||
|SITE= <scene name='pdbsite=NA BINDING SITE:Umq+Binding+Site+For+Chain+F'>NA BINDING SITE</scene> | |SITE= <scene name='pdbsite=NA BINDING SITE:Umq+Binding+Site+For+Chain+F'>NA BINDING SITE</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=LHG:1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE'>LHG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=UMQ:UNDECYL-MALTOSIDE'>UMQ</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bl2 OCA], [http://www.ebi.ac.uk/pdbsum/2bl2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bl2 RCSB]</span> | |||
}} | }} | ||
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[[Category: Walker, J E.]] | [[Category: Walker, J E.]] | ||
[[Category: Yamato, I.]] | [[Category: Yamato, I.]] | ||
[[Category: hydrogen ion transport]] | [[Category: hydrogen ion transport]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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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 Mon Mar 31 02:07:58 2008'' |
Revision as of 02:08, 31 March 2008
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, resolution 2.10Å | |||||||
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Sites: | |||||||
Ligands: | , , | ||||||
Activity: | H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
THE MEMBRANE ROTOR OF THE V-TYPE ATPASE FROM ENTEROCOCCUS HIRAE
OverviewOverview
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 StructureAbout this Structure
2BL2 is a Single protein structure of sequence from Enterococcus hirae. Full crystallographic information is available from OCA.
ReferenceReference
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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