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4YDS

FlaH from Sulfolobus acidocaldarius with ATP and Mg-Ion

Summary for 4YDS
Entry DOI10.2210/pdb4yds/pdb
Related2DR3
DescriptorFlagella-related protein H, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordsreca superfamily atpase, hydrolase
Biological sourceSulfolobus acidocaldarius
Total number of polymer chains1
Total formula weight25907.30
Authors
Reindl, S.,Arvai, A.S.,Tainer, J.A. (deposition date: 2015-02-23, release date: 2015-11-11, Last modification date: 2023-09-27)
Primary citationChaudhury, P.,Neiner, T.,D'Imprima, E.,Banerjee, A.,Reindl, S.,Ghosh, A.,Arvai, A.S.,Mills, D.J.,van der Does, C.,Tainer, J.A.,Vonck, J.,Albers, S.V.
The nucleotide-dependent interaction of FlaH and FlaI is essential for assembly and function of the archaellum motor.
Mol.Microbiol., 99:674-685, 2016
Cited by
PubMed Abstract: The motor of the membrane-anchored archaeal motility structure, the archaellum, contains FlaX, FlaI and FlaH. FlaX forms a 30 nm ring structure that acts as a scaffold protein and was shown to interact with the bifunctional ATPase FlaI and FlaH. However, the structure and function of FlaH has been enigmatic. Here we present structural and functional analyses of isolated FlaH and archaellum motor subcomplexes. The FlaH crystal structure reveals a RecA/Rad51 family fold with an ATP bound on a conserved and exposed surface, which presumably forms an oligomerization interface. FlaH does not hydrolyze ATP in vitro, but ATP binding to FlaH is essential for its interaction with FlaI and for archaellum assembly. FlaH interacts with the C-terminus of FlaX, which was earlier shown to be essential for FlaX ring formation and to mediate interaction with FlaI. Electron microscopy reveals that FlaH assembles as a second ring inside the FlaX ring in vitro. Collectively these data reveal central structural mechanisms for FlaH interactions in mediating archaellar assembly: FlaH binding within the FlaX ring and nucleotide-regulated FlaH binding to FlaI form the archaellar basal body core.
PubMed: 26508112
DOI: 10.1111/mmi.13260
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

226707

数据于2024-10-30公开中

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