2YHS: E. coli SRP receptor FtsY

Structure of the E. coli SRP receptor FtsY. Determined by X-ray diffraction at 1.6 Å resolution. Released 18 May 2011.

Method: X-ray diffraction
Resolution: 1.6 Å
Organism: ESCHERICHIA COLI
Chains: 1
Atoms: 2,656
Mol. weight: 55.71 kDa
Released: 18 May 2011

Explore 2YHS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2YHS contains 18 α-helices and 11 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: 18 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	192-202	11
α-helix	204-207	4
α-helix	213-218	6
β-strand	222	1	1
α-helix	225-237	13
α-helix	242-259	18
β-strand	263	1	1
α-helix	264-266	3
α-helix	267-280	14
β-strand	283	1	2
β-strand	294-299	6	2
α-helix	306-319	14
β-strand	324-327	4	2
α-helix	334-347	14
β-strand	351-352	2	2
α-helix	360-373	14
β-strand	378-381	4	2
α-helix	390-405	16
β-strand	414-420	7	2
α-helix	421-423	3
α-helix	425-437	13
β-strand	442-446	5	2
α-helix	448-450	3
α-helix	456-464	9
β-strand	468-472	5	2
α-helix	477-479	3
β-strand	480-482	3	2
α-helix	483	1
α-helix	485-493	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cell division protein ftsy	A	protein	503	ESCHERICHIA COLI	P10121 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2YHS_1 CELL DIVISION PROTEIN FTSY (chains A)
MAKEKKRGFFSWLGFGQKEQTPEKETEVQNEQPVVEEIVQAQEPVKASEQAVEEQPQAHT
EAEAETFAADVVEVTEQVAESEKAQPEAEVVAQPEPVVEETPEPVAIEREELPLPEDVNA
EAVSPEEWQAEAETVEIVEAAEEEAAKEEITDEELETALAAEAAEEAVMVVPPAEEEQPV
EEIAQEQEKPTKEGFFARLKRSLLKTKENLGSGFISLFRGKKIDDDLFEELEEQLLIADV
GVETTRKIITNLTEGASRKQLRDAEALYGLLKEEMGEILAKVDEPLNVEGKAPFVILMVG
VNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADS
ASVIFDAIQAAKARNIDVLIADTAGRLQNKSHLMEELKKIVRVMKKLDVEAPHEVMLTID
ASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERIEDL
RPFKADDFIEALFAREDHHHHHH

Primary citation

Lipids Trigger a Conformational Switch that Regulates Signal Recognition Particle (Srp)-Mediated Protein Targeting. Stjepanovic, G., Kapp, K., Bange, G. et al. J Biol Chem (2011) 286:23489. DOI 10.1074/JBC.M110.212340 · PubMed

Other PDB entries of the same protein (UniProt P10121 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6N9B 1.22 Å, FtsY-NG ultra high-resolution
6N5J 1.37 Å, FtsY-NG high-resolution
6CQP 1.45 Å, High resolution crystal structure of FtsY-NG domain of E. coli
6N5I 1.5 Å, FtsY-NG high-resolution
6NC1 1.6 Å, FtsY-NG high-resolution
6NC4 1.6 Å, FtsY-NG high-resolution
5NIY 1.7 Å, Signal recognition particle-docking protein FtsY
6CS8 1.75 Å, High resolution crystal structure of FtsY-NG domain of E. coli
6CVD 1.78 Å, High resolution crystal structure of FtsY-NG domain of E. coli bound to fragment 1
6DLX 1.85 Å, FtsY-NG domain bound to fragment 3.
6N6N 1.88 Å, FtsY-NG high-resolution
2QY9 1.9 Å, Structure of the NG+1 construct of the E. coli SRP receptor FtsY

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