5AJI: MscS D67R1 high resolution

MscS D67R1 high resolution. Determined by X-ray diffraction at 2.99 Å resolution. Released 8 Jul 2015.

Method: X-ray diffraction
Resolution: 2.99 Å
Organism: ESCHERICHIA COLI
Chains: 7
Atoms: 13,963
Mol. weight: 219.18 kDa
Ligands: D10, HEX, OCT
Released: 8 Jul 2015

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

Secondary structure: helices and β-sheets

5AJI contains 49 α-helices and 63 β-strands across 7 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: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	22-58	37
α-helix	63-87	25
α-helix	93-127	35
β-strand	135-138	4	1
β-strand	142-148	7	1
β-strand	152-156	5	1
β-strand	162-166	5	1
α-helix	167-172	6
β-strand	175-177	3	1
β-strand	183-192	10	2
α-helix	198-211	14
β-strand	221-228	8	2
β-strand	233-242	10	2
α-helix	243-264	22
α-helix	269-271	3
β-strand	272-279	8	3

Chains B and C: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	27-58	32
α-helix	63-87	25
α-helix	93-127	35
β-strand	135-138	4	1
β-strand	142-148	7	1
β-strand	152-156	5	1
β-strand	162-166	5	1
α-helix	167-172	6
β-strand	175-177	3	1
β-strand	183-192	10	4
α-helix	198-211	14
β-strand	221-228	8	4
β-strand	233-242	10	4
α-helix	243-264	22
α-helix	269-271	3
β-strand	272-278	7	3

Chain D: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	22-58	37
α-helix	63-87	25
α-helix	93-127	35
β-strand	135-138	4	1
β-strand	142-148	7	1
β-strand	152-156	5	1
β-strand	162-166	5	1
α-helix	167-172	6
β-strand	175-177	3	1
β-strand	183-192	10	6
α-helix	198-211	14
β-strand	221-228	8	6
β-strand	233-242	10	6
α-helix	243-264	22
α-helix	269-271	3
β-strand	272-278	7	3

Chain E: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	22-58	37
α-helix	63-87	25
α-helix	93-127	35
β-strand	135-138	4	1
β-strand	142-148	7	1
β-strand	152-156	5	1
β-strand	162-166	5	1
α-helix	167-172	6
β-strand	175-177	3	1
β-strand	183-192	10	7
α-helix	198-211	14
β-strand	221-228	8	7
β-strand	233-242	10	7
α-helix	243-264	22
α-helix	269-271	3
β-strand	272-277	6	3

Chain F: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	27-58	32
α-helix	63-88	26
α-helix	93-127	35
β-strand	135-138	4	1
β-strand	142-148	7	1
β-strand	152-156	5	1
β-strand	162-166	5	1
α-helix	167-172	6
β-strand	175-177	3	1
β-strand	183-192	10	8
α-helix	198-211	14
β-strand	221-228	8	8
β-strand	233-242	10	8
α-helix	243-264	22
α-helix	269-271	3
β-strand	272-279	8	3

Chain G: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	27-58	32
α-helix	63-87	25
α-helix	93-127	35
β-strand	135-138	4	1
β-strand	142-148	7	1
β-strand	152-156	5	1
β-strand	162-166	5	1
α-helix	167-172	6
β-strand	175-177	3	1
β-strand	183-192	10	9
α-helix	198-211	14
β-strand	221-228	8	9
β-strand	233-242	10	9
α-helix	243-264	22
α-helix	269-271	3
β-strand	272-277	6	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Small-conductance mechanosensitive channel	A, B, C, D, E, F, G	protein	286	ESCHERICHIA COLI	P0C0S1 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G), FASTA

>5AJI_1 SMALL-CONDUCTANCE MECHANOSENSITIVE CHANNEL (chains A, B, C, D, E, F, G)
MEDLNVVDSINGAGSWLVANQALLLSYAVNIVAALAIIIVGLIIARMISNAVNRLMISRK
IDATVACFLSALVRYGIIAFTLIAALGRVGVQTASVIAVLGAAGLAVGLALQGSLSNLAA
GVLLVMFRPFRAGEYVDLGGVAGTVLSVQIFSTTMRTADGKIIVIPNGKIIAGNIINFSR
EPVRRNEFIIGVAYDSDIDQVKQILTNIIQSEDRILKDREMTVRLNELGASSINFVVRVW
SNSGDLQNVYWDVLERIKREFDAAGISFPYPQMDVNFKRVKEDKAA

Ligands and cofactors

ID	Name	Formula	Copies
D10	Decane	C10 H22	3
HEX	Hexane	C6 H14	10
OCT	N-octane	C8 H18	2

Primary citation

The Role of Lipids in Mechanosensation. Pliotas, C., Dahl, A.C.E., Rasmussen, T. et al. Nat Struct Mol Biol (2015) 22:991. DOI 10.1038/NSMB.3120 · PubMed

Other PDB entries of the same protein (UniProt P0C0S1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7ONJ 2.3 Å, Mechanosensitive channel MscS solubilized with LMNG in open conformation
9E68 2.5 Å, Cryo-EM structure of MscS/YnaI chimera in DOPC nanodiscs
7OOA 2.7 Å, Mechanosensitive channel MscS solubilized with LMNG in open conformation with added lipid
9H2S 2.7 Å, a YnaI-MscS chimera in a closed conformation purified in DDM with additional lipids…
9H2V 2.8 Å, a YnaI-MscS chimera in an open conformation purified in DDM showing ligand-filled pockets
6RLD 2.9 Å, Structure of the mechanosensitive channel mscs embedded in the membrane bilayer
6PWN 3.1 Å, MscS Nanodisc with N-terminal His-Tag
7OO0 3.1 Å, Mechanosensitive channel MscS solubilized with DDM in open conformation
7OO6 3.1 Å, Mechanosensitive channel MscS solubilized with DDM in closed conformation with added lipid
8DDJ 3.1 Å, Open MscS in PC14.1 Nanodiscs
6VYK 3.2 Å, Cryo-EM structure of mechanosensitive channel MscS in PC-18:1 nanodiscs
6UZH 3.3 Å, Cryo-EM structure of mechanosensitive channel MscS reconstituted into peptidiscs

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