8GA1: CLC-ec1 R230C/L249C/C85A at pH 4.5 100mM Cl Swap

CLC-ec1 R230C/L249C/C85A at pH 4.5 100mM Cl Swap. Determined by electron microscopy at 2.6 Å resolution. Released 7 Feb 2024.

Method: Electron microscopy
Resolution: 2.6 Å
Organism: Escherichia coli
Chains: 2
Atoms: 6,781
Mol. weight: 98.38 kDa
Released: 7 Feb 2024

Explore 8GA1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8GA1 contains 50 α-helices and 8 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: 24 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	14-25	12
α-helix	33-66	34
α-helix	75-100	26
α-helix	102-104	3
β-strand	106	1	1
α-helix	109-115	7
α-helix	124-140	17
β-strand	146	1	2
α-helix	148-164	17
α-helix	171-190	20
α-helix	193-202	10
α-helix	215-232	18
α-helix	254-284	31
α-helix	288-304	17
α-helix	310-312	3
α-helix	319-322	4
α-helix	330-348	19
β-strand	353	1	1
β-strand	355	1	2
α-helix	357-378	22
α-helix	387-392	6
α-helix	397	1
α-helix	398-402	5
α-helix	405-416	12
α-helix	419-421	3
α-helix	422-438	17
α-helix	441-443	3
α-helix	444-458	15

Chain B: 26 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	14-26	13
α-helix	33-66	34
α-helix	75-99	25
α-helix	102-104	3
β-strand	106	1	3
α-helix	109-115	7
α-helix	124-140	17
β-strand	146	1	4
α-helix	149-164	16
α-helix	171-190	20
α-helix	193-199	7
α-helix	200-204	5
α-helix	215-231	17
α-helix	252-284	33
α-helix	288-307	20
α-helix	310-312	3
α-helix	319-322	4
α-helix	331-348	18
β-strand	353	1	3
β-strand	355	1	4
α-helix	357-378	22
α-helix	380-382	3
α-helix	386-394	9
α-helix	396-397	2
α-helix	398-402	5
α-helix	405-416	12
α-helix	419-421	3
α-helix	422-438	17
α-helix	441-443	3
α-helix	444-459	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
H(+)/Cl(-) exchange transporter ClcA	A, B	protein	461	Escherichia coli	P37019 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8GA1_1 H(+)/Cl(-) exchange transporter ClcA (chains A, B)
MKTDTPSLETPQAARLRRRQLIRQLLERDKTPLAILFMAAVVGTLVGLAAVAFDKGVAWL
QNQRMGALVHTADNYPLLLTVAFLASAVLAMFGYFLVRKYAPEAGGSGIPEIEGALEDQR
PVRWWRVLPVKFFGGLGTLGGGMVLGREGPTVQIGGNIGRMVLDIFRLKGDEARHTLLAT
GAAAGLAAAFNAPLAGILFIIEEMRPQFRYTLISIKAVFIGVIMSTIMYCIFNHEVALID
VGKLSDAPCNTLWLYLILGIIFGIFGPIFNKWVLGMQDLLHRVHGGNITKWVLMGGAIGG
LCGLLGFVAPATSGGGFNLIPIATAGNFSMGMLVFIFVARVITTLLCFSSGAPGGIFAPM
LALGTVLGTAFGMVAVELFPQYHLEAGTFAIAGMGALLAASIRAPLTGIILVLEMTDNYQ
LILPMIITGLGATLLAQFTGGKPLYSAILARTLAKQEAEQL

Primary citation

Structural basis of pH-dependent activation in a CLC transporter. Fortea, E., Lee, S., Chadda, R. et al. Nat Struct Mol Biol (2024) 31:644-656. DOI 10.1038/s41594-023-01210-5 · PubMed

Other PDB entries of the same protein (UniProt P37019 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4ENE 2.4 Å, Structure of the N- and C-terminal trimmed ClC-ec1 Cl-/H+ antiporter and Fab Complex
1OTS 2.51 Å, Structure of the Escherichia coli ClC Chloride channel and Fab Complex
8GA5 2.6 Å, CLC-ec1 L25C/A450C/C85A at pH 4.5 100mM Cl Intermediate
6V2J 2.62 Å, Crystal structure of ClC-ec1 triple mutant (E113Q, E148Q, E203Q)
6ADB 2.69 Å, Crystal structure of the E148N mutant CLC-ec1 in 20mM bromide
3DET 2.8 Å, Structure of the E148A, Y445A doubly ungated mutant of E.coli CLC_Ec1, Cl-/H+ antiporter
4KKL 2.85 Å, Structure of the E148A mutant of CLC-ec1 delta NC construct in 100mM fluoride
4KK8 2.86 Å, Structure of the E148Q mutant of CLC-ec1 deltaNC construct in 100mM fluoride
4KJQ 2.88 Å, Structure of the CLC-ec1 deltaNC construct in 100mM fluoride
3EJZ 2.9 Å, Structure of E203V mutant E.coli Cl-/H+ exchanger, CLC-ec1
7CVT 2.9 Å, Crystal structure of the C85A/L194A/H234C mutant CLC-ec1 with Fab fragment
8GAH 2.9 Å, CLC-ec1 L25C/A450C/C85A at pH 4.5 100mM Cl Twist

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