2VH1: Bacterial cell division protein FtsQ from E.coli

Crystal structure of bacterial cell division protein FtsQ from E.coli. Determined by X-ray diffraction at 2.7 Å resolution. Released 11 Mar 2008.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: ESCHERICHIA COLI
Chains: 2
Atoms: 3,234
Mol. weight: 50.59 kDa
Released: 11 Mar 2008

Explore 2VH1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2VH1 contains 12 α-helices and 24 β-strands across 2 chains. 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: 6 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	59-63	5	1
α-helix	71-79	9
α-helix	87-89	3
α-helix	92-102	11
β-strand	106-114	9	1
β-strand	118-125	8	1
β-strand	128-132	5	2
β-strand	136-139	4	2
β-strand	144-146	3	2
α-helix	149-151	3
β-strand	159-161	3	2
α-helix	167-182	16
β-strand	190-193	4	2
β-strand	199-202	4	2
β-strand	208-212	5	2
α-helix	216-236	21
β-strand	239-248	10	2
β-strand	251-258	8	2

Chain B: 6 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	59-63	5	3
α-helix	71-79	9
α-helix	87-89	3
α-helix	92-102	11
β-strand	106-114	9	3
β-strand	118-125	8	3
β-strand	128-132	5	2
β-strand	136-139	4	2
β-strand	144-145	2	2
β-strand	159-161	3	2
α-helix	167-182	16
β-strand	190-193	4	2
β-strand	199-202	4	2
β-strand	208-212	5	2
α-helix	216-230	15
α-helix	231-233	3
β-strand	243-245	3	2
β-strand	251-255	5	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cell division protein ftsq	A, B	protein	220	ESCHERICHIA COLI	P06136 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2VH1_1 CELL DIVISION PROTEIN FTSQ (chains A, B)
MSKLVLTGERHYTRNDDIRQSILALGEPGTFMTQDVNIIQTQIEQRLPWIKQVSVRKQWP
DELKIHLVEYVPIARWNDQHMVDAEGNTFSVPPERTSKQVLPMLYGPEGSANEVLQGYRE
MGQMLAKDRFTLKEAAMTARRSWQLTLNNDIKLNLGRGDTMKRLARFVELYPVLQQQAQT
DGKRISYVDLRYDSGAAVGWAPLPPEESTQQQNQAQAEQQ

Primary citation

Structural and Mutational Analysis of Cell Division Protein Ftsq. van den Ent, F., Vinkenvleugel, T., Ind, A. et al. Mol Microbiol (2008) 68:110. DOI 10.1111/J.1365-2958.2008.06141.X · PubMed

Other PDB entries of the same protein (UniProt P06136 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6H9N 2.6 Å, Complex of the periplasmic domains of bacterial cell division proteins FtsQ and FtsB
6H9O 2.8 Å, Complex of the periplasmic domains of bacterial cell division proteins FtsQ and FtsB
5Z2W 3.0 Å, Crystal structure of the bacterial cell division protein FtsQ and FtsB
8HHF 3.04 Å, The bacterial divisome protein complex FtsB-FtsL-FtsQ
8HHG 3.1 Å, The bacterial divisome protein complex FtsB-FtsL-FtsQ
8YA3 3.27 Å, Structure of the SecA-SecY complex with the substrate FtsQ-LacY(+7C) treated with DTT
8Y9Y 3.29 Å, Structure of the SecA-SecY complex with the substrate FtsQ-LacY(+1C)
8HHH 3.3 Å, The bacterial divisome protein complex FtsB-FtsL-FtsQ
8YA2 3.84 Å, Structure of the SecA-SecY complex with the substrate FtsQ-LacY(+20C)
4UE4 7.0 Å, Structural basis for targeting and elongation arrest of Bacillus signal recognition…

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