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8B24

Time-resolved structure of K+-dependent Na+-PPase from Thermotoga maritima 3600-seconds post reaction initiation with Na+

Summary for 8B24
Entry DOI10.2210/pdb8b24/pdb
DescriptorK(+)-stimulated pyrophosphate-energized sodium pump, DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
Functional Keywordsmembrane bound pyrophosphatase, membrane protein, enzyme, complex
Biological sourceThermotoga maritima
Total number of polymer chains2
Total formula weight157080.32
Authors
Strauss, J.,Vidilaseris, K.,Goldman, A. (deposition date: 2022-09-12, release date: 2024-01-17, Last modification date: 2024-04-10)
Primary citationStrauss, J.,Wilkinson, C.,Vidilaseris, K.,de Castro Ribeiro, O.M.,Liu, J.,Hillier, J.,Wichert, M.,Malinen, A.M.,Gehl, B.,Jeuken, L.J.,Pearson, A.R.,Goldman, A.
Functional and structural asymmetry suggest a unifying principle for catalysis in membrane-bound pyrophosphatases.
Embo Rep., 25:853-875, 2024
Cited by
PubMed: 38182815
DOI: 10.1038/s44319-023-00037-x
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4.53 Å)
Structure validation

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