5AEM: T131 N-terminal TPR array

Structure of t131 N-terminal TPR array. Determined by X-ray diffraction at 3.4 Å resolution. Released 24 Jun 2015.

Method: X-ray diffraction
Resolution: 3.4 Å
Organism: SACCHAROMYCES CEREVISIAE S288C
Chains: 1
Atoms: 3,379
Mol. weight: 52.37 kDa
Released: 24 Jun 2015

Explore 5AEM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5AEM contains 30 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 30 helices, 0 β-strands

Element	Residues	Length
α-helix	132-141	10
α-helix	145-154	10
α-helix	162-175	14
α-helix	178-191	14
α-helix	196-208	13
α-helix	212-225	14
α-helix	230-242	13
α-helix	246-259	14
α-helix	264-276	13
α-helix	280-311	32
α-helix	343-349	7
α-helix	352-354	3
α-helix	357-370	14
α-helix	374-387	14
α-helix	388-390	3
α-helix	396-399	4
α-helix	408-411	4
α-helix	414-418	5
α-helix	421-424	4
α-helix	432-443	12
α-helix	448-455	8
α-helix	456-460	5
α-helix	467-479	13
α-helix	483-490	8
α-helix	491-494	4
α-helix	497-499	3
α-helix	502-514	13
α-helix	518-531	14
α-helix	536-547	12
α-helix	555-560	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transcription factor tau 131 kda subunit	A	protein	447	SACCHAROMYCES CEREVISIAE S288C	P33339 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5AEM_1 TRANSCRIPTION FACTOR TAU 131 KDA SUBUNIT (chains A)
GAMVLDPEVAQLLSQANEAFVRNDLQVAERLFNEVIKKDARNFAAYETLGDIYQLQGRLN
DCCNSWFLAAHLNASDWEFWKIVAILSADLDHVRQAIYCFSRVISLNPMEWESIYRRSML
YKKTGQLARALDGFQRLYMYNPYDANILRELAILYVDYDRIEDSIELYMKVFNANVERRE
AILAALENALDSSDEESAAEGEDADEKEPLEQDEDRQMFPDINWKKIDAKYKCIPFDWSS
LNILAELFLKLAVSEVDGIKTIKKCARWIQRRESQTFWDHVPDDSEFDNRRFKNSTFDSL
LAAEKEKSYNIPIDIRVRLGLLRLNTDNLVEALNHFQCLYDETFSDVADLYFEAATALTR
AEKYKEAIDFFTPLLSLEEWRTTDVFKPLARCYKEIESYETAKEFYELAIKSEPDDLDIR
VSLAEVYYRLNDPETFKHMLVDVVEMR

Primary citation

Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly. Male, G., von Appen, A., Glatt, S. et al. Nat Commun (2015) 6:7387-7387. DOI 10.1038/ncomms8387 · PubMed

Other PDB entries of the same protein (UniProt P33339 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6YJ6 3.1 Å, Structure of the TFIIIC subcomplex tauA
5AIO 3.15 Å, Crystal structure of t131 N-terminal TPR array
9GCK 3.7 Å, yeast TFIIIC TauA subcomplex bound to a tRNA gene
8FFZ 3.8 Å, TFIIIA-TFIIIC-Brf1-TBP complex bound to 5S rRNA gene

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