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4IDP

human atlastin-1 1-446, N440T, GppNHp

Summary for 4IDP
Entry DOI10.2210/pdb4idp/pdb
Related3Q5D 3Q5E 4IDN 4IDO 4IDQ
DescriptorAtlastin-1, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordsgtpase, gtp/gdp binding, hydrolase
Biological sourceHomo sapiens (human)
Cellular locationEndoplasmic reticulum membrane; Multi-pass membrane protein: Q8WXF7
Total number of polymer chains4
Total formula weight209226.13
Authors
Byrnes, L.J.,Singh, A.,Szeto, K.,Benvin, N.M.,O'Donnell, J.P.,Zipfel, W.R.,Sondermann, H. (deposition date: 2012-12-12, release date: 2013-01-09, Last modification date: 2024-10-16)
Primary citationByrnes, L.J.,Singh, A.,Szeto, K.,Benvin, N.M.,O'Donnell, J.P.,Zipfel, W.R.,Sondermann, H.
Structural basis for conformational switching and GTP loading of the large G protein atlastin.
Embo J., 32:369-384, 2013
Cited by
PubMed Abstract: Atlastin, a member of the dynamin superfamily, is known to catalyse homotypic membrane fusion in the smooth endoplasmic reticulum (ER). Recent studies of atlastin have elucidated key features about its structure and function; however, several mechanistic details, including the catalytic mechanism and GTP hydrolysis-driven conformational changes, are yet to be determined. Here, we present the crystal structures of atlastin-1 bound to GDP·AlF(4)(-) and GppNHp, uncovering an intramolecular arginine finger that stimulates GTP hydrolysis when correctly oriented through rearrangements within the G domain. Utilizing Förster Resonance Energy Transfer, we describe nucleotide binding and hydrolysis-driven conformational changes in atlastin and their sequence. Furthermore, we discovered a nucleotide exchange mechanism that is intrinsic to atlastin's N-terminal domains. Our results indicate that the cytoplasmic domain of atlastin acts as a tether and homotypic interactions are timed by GTP binding and hydrolysis. Perturbation of these mechanisms may be implicated in a group of atlastin-associated hereditary neurodegenerative diseases.
PubMed: 23334294
DOI: 10.1038/emboj.2012.353
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.587 Å)
Structure validation

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