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8Q30

Sulfolobus acidocaldarius AAP filament.

This is a non-PDB format compatible entry.
Summary for 8Q30
Entry DOI10.2210/pdb8q30/pdb
EMDB information18119
DescriptorDUF4352 domain-containing protein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 6-deoxy-6-sulfo-beta-D-glucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordscell surface appendage, n-glycosylation, protein fibril
Biological sourceSulfolobus acidocaldarius
Total number of polymer chains72
Total formula weight1108644.14
Authors
Isupov, M.N.,Gaines, M.,Daum, B.,McLaren, M. (deposition date: 2023-08-03, release date: 2024-03-06, Last modification date: 2024-10-23)
Primary citationGaines, M.C.,Sivabalasarma, S.,Isupov, M.N.,Haque, R.U.,McLaren, M.,Hanus, C.,Gold, V.A.M.,Albers, S.V.,Daum, B.
CryoEM reveals the structure of an archaeal pilus involved in twitching motility.
Nat Commun, 15:5050-5050, 2024
Cited by
PubMed Abstract: Amongst the major types of archaeal filaments, several have been shown to closely resemble bacterial homologues of the Type IV pili (T4P). Within Sulfolobales, member species encode for three types of T4P, namely the archaellum, the UV-inducible pilus system (Ups) and the archaeal adhesive pilus (Aap). Whereas the archaellum functions primarily in swimming motility, and the Ups in UV-induced cell aggregation and DNA-exchange, the Aap plays an important role in adhesion and twitching motility. Here, we present a cryoEM structure of the Aap of the archaeal model organism Sulfolobus acidocaldarius. We identify the component subunit as AapB and find that while its structure follows the canonical T4P blueprint, it adopts three distinct conformations within the pilus. The tri-conformer Aap structure that we describe challenges our current understanding of pilus structure and sheds new light on the principles of twitching motility.
PubMed: 38877033
DOI: 10.1038/s41467-024-45831-w
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.22 Å)
Structure validation

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