4L4U: Transcriptional regulator

Crystal structure of construct containing A. aeolicus NtrC1 receiver, central and DNA binding domains. Determined by X-ray diffraction at 2.2 Å resolution. Released 28 Aug 2013.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Aquifex aeolicus
Chains: 1
Atoms: 3,276
Mol. weight: 51.23 kDa
Released: 28 Aug 2013

Explore 4L4U in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4L4U contains 22 α-helices and 19 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: 22 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	-6--4	3
β-strand	2-6	5	1
α-helix	10-22	13
β-strand	26-30	5	1
α-helix	33-42	10
β-strand	47-51	5	1
β-strand	53	1	2
β-strand	58	1	2
α-helix	59-69	11
β-strand	74-80	7	1
α-helix	85-92	8
β-strand	97-101	5	1
α-helix	105-134	30
α-helix	144-155	12
β-strand	163-166	4	3
α-helix	174-183	10
β-strand	191-194	4	3
α-helix	196-198	3
α-helix	201-209	9
β-strand	210-211	2	4
β-strand	223-224	2	4
α-helix	226-229	4
β-strand	234-237	4	3
α-helix	240-242	3
α-helix	245-256	12
β-strand	259-261	3	5
β-strand	263	1	4
β-strand	268-270	3	5
β-strand	274-279	6	3
α-helix	283-288	6
α-helix	294-301	8
β-strand	304-306	3	3
α-helix	307-309	3
α-helix	310-312	3
α-helix	314-316	3
α-helix	317-331	15
β-strand	338-339	2	6
α-helix	341-349	9
α-helix	355-368	14
β-strand	374-375	2	6
α-helix	377-381	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transcriptional regulator (NtrC family)	A	protein	447	Aquifex aeolicus	O67198 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4L4U_1 Transcriptional regulator (NtrC family) (chains A)
GLVPRGSHMNVLVIEDDKVFRGLLEEYLSMKGIKVESAERGKEAYKLLSEKHFNVVLLDL
LLPDVNGLEILKWIKERSPETEVIVITGHGTIKTAVEAMKMGAYDFLTKPCMLEEIELTI
NKAIEHRKLRKENELLRREKDLKEEEYVFESPKMKEILEKIKKISCAECPVLITGESGVG
KEVVARLIHKSSDRSKEPFVALNVASIPRDIFEAELFGYEKGAFTGAVSSKEGFFELADG
GTLFLDEIGELSLEAQAKLLRVIESGKFYRLGGRKEIEVNVRILAATNRNIKELVKEGKF
REDLYYRLGVIEIEIPPLRERKEDIIPLANHFLKKFSRKYAKEVEGFTKSAQELLLSYPW
YGNVRELKNVIERAVLFSEGKFIDRGELSCLVNSKGIKNKHKSIKEIEKEEIIKVLKEVN
FNKKLASEILGIPLRTLYRRLKEYGIE

Primary citation

Structure, function, and tethering of DNA-binding domains in sigma (54) transcriptional activators. Vidangos, N., Maris, A.E., Young, A. et al. Biopolymers (2013) 99:1082-1096. DOI 10.1002/bip.22333 · PubMed

Other PDB entries of the same protein (UniProt O67198 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4L5E 1.34 Å, Crystal structure of A. aeolicus NtrC1 DNA binding domain
1NY5 2.4 Å, Crystal structure of sigm54 activator (AAA+ ATPase) in the inactive state
9MSF 2.6 Å, de novo SigN RNA polymerase transcription initiation intermediate with post-catalytic…
3M0E 2.63 Å, Crystal structure of the ATP-bound state of Walker B mutant of NtrC1 ATPase domain
9MSE 2.7 Å, de novo SigN RNA polymerase transcription initiation intermediate with pre-catalytic…
9MSG 2.7 Å, De novo SigN RNA polymerase transcription initiation intermediate with bound SigN-RII
1ZY2 3.03 Å, Crystal structure of the phosphorylated receiver domain of the transcription regulator…
1NY6 3.1 Å, Crystal structure of sigm54 activator (AAA+ ATPase) in the active state
4LZZ 3.21 Å, Nucleotide-induced asymmetry within atpase activator ring drives s54-RNAP interaction…
4LY6 3.6 Å, Nucleotide-induced asymmetry within ATPase activator ring drives s54-RNAP interaction…
4BT1 16.0 Å, MuB is an AAAplus ATPase that forms helical filaments to control target selection for…
4BT0 17.0 Å, MuB is an AAAplus ATPase that forms helical filaments to control target selection for…

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