7CVT: H/Cl exchange transporter ClcA

Crystal structure of the C85A/L194A/H234C mutant CLC-ec1 with Fab fragment. Determined by X-ray diffraction at 2.9 Å resolution. Released 1 Sept 2021.

Method: X-ray diffraction
Resolution: 2.9 Å
Organisms: Escherichia coli MS 198-1, Mus musculus
Chains: 6
Atoms: 13,248
Mol. weight: 194.49 kDa
Released: 1 Sept 2021

Explore 7CVT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7CVT contains 75 α-helices and 90 β-strands across 6 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: 26 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	18-25	8
α-helix	33-67	35
α-helix	75-100	26
α-helix	102-104	3
α-helix	109-116	8
α-helix	124-140	17
β-strand	146	1	1
α-helix	148-165	18
α-helix	171-190	20
α-helix	193-199	7
α-helix	200-204	5
α-helix	215-230	16
α-helix	249-251	3
α-helix	252-284	33
α-helix	288-308	21
α-helix	310-312	3
α-helix	319-324	6
α-helix	330-348	19
β-strand	355	1	1
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	444-458	15

Chain B: 26 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	18-25	8
α-helix	33-67	35
α-helix	75-100	26
α-helix	102-104	3
α-helix	109-116	8
α-helix	124-140	17
β-strand	146	1	2
α-helix	148-165	18
α-helix	171-190	20
α-helix	193-199	7
α-helix	200-204	5
α-helix	215-231	17
α-helix	249-251	3
α-helix	252-284	33
α-helix	288-308	21
α-helix	310-312	3
α-helix	319-324	6
α-helix	330-348	19
β-strand	355	1	2
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	444-458	15

Chain C: 6 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	3
β-strand	11-12	2	4
β-strand	18-25	8	3
β-strand	34-39	6	5
β-strand	45-51	7	5
β-strand	58-60	3	5
β-strand	68-73	6	3
β-strand	78-83	6	3
α-helix	88-90	3
β-strand	92-100	9	5
β-strand	107-111	5	5
β-strand	115-117	3	5
β-strand	118-119	2	4
α-helix	123-124	2
β-strand	125	1	6
β-strand	128-132	5	7
α-helix	133-135	3
β-strand	143-153	11	7
β-strand	154	1	6
β-strand	159-162	4	8
α-helix	163-165	3
β-strand	171-173	3	7
α-helix	174-176	3
β-strand	177-179	3	7
β-strand	182-192	11	7
β-strand	201-207	7	8
α-helix	208-210	3
β-strand	212-218	7	8

Chain D: 5 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	9
β-strand	10-13	4	10
β-strand	19-25	7	9
β-strand	33-37	5	10
β-strand	44-48	5	10
β-strand	52-53	2	10
α-helix	54	1
β-strand	61-66	6	9
β-strand	69-74	6	9
α-helix	79-81	3
β-strand	83-89	7	10
β-strand	96-97	2	10
β-strand	98	1	9
β-strand	101-105	5	10
β-strand	110	1	11
β-strand	113-117	5	12
α-helix	118-120	3
α-helix	121-126	6
β-strand	128-136	9	12
β-strand	139	1	11
β-strand	144-149	6	13
β-strand	152-154	3	13
β-strand	158-162	5	12
β-strand	173-181	9	12
α-helix	182-186	5
β-strand	190-196	7	13
β-strand	204-209	6	13

Chain E: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	14
β-strand	10-12	3	15
β-strand	17-25	9	14
β-strand	34-39	6	15
β-strand	45-51	7	15
β-strand	58-60	3	15
β-strand	68-73	6	14
β-strand	78-84	7	14
α-helix	88-90	3
β-strand	92-100	9	15
β-strand	107-111	5	15
β-strand	115-119	5	15
β-strand	125	1	16
α-helix	126-127	2
β-strand	128-132	5	17
β-strand	143-153	11	17
β-strand	154	1	16
β-strand	159-162	4	18
α-helix	163-165	3
β-strand	171-173	3	17
α-helix	174-176	3
β-strand	177-179	3	17
β-strand	182-192	11	17
α-helix	193-195	3
β-strand	201-207	7	18
α-helix	208-210	3
β-strand	212-218	7	18

Chain F: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	19
β-strand	10-13	4	20
β-strand	19-25	7	19
β-strand	33-37	5	20
β-strand	44-48	5	20
β-strand	52-53	2	20
α-helix	54	1
β-strand	61-66	6	19
β-strand	69-74	6	19
α-helix	79-81	3
β-strand	83-89	7	20
β-strand	96-97	2	20
β-strand	101-105	5	20
β-strand	110	1	21
β-strand	113-117	5	22
α-helix	118-120	3
α-helix	121-124	4
β-strand	128-138	11	22
β-strand	139	1	21
β-strand	144-149	6	23
β-strand	154	1	23
β-strand	158-162	5	22
α-helix	163-166	4
β-strand	172-181	10	22
α-helix	182-186	5
β-strand	190-197	8	23
β-strand	200-209	10	23

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
H(+)/Cl(-) exchange transporter ClcA	A, B	protein	473	Escherichia coli MS 198-1	P37019 (AlphaFold model)
antibody Fab fragment heavy chain	C, E	protein	222	Mus musculus
antibody Fab fragment light chain	D, F	protein	211	Mus musculus

Sequence of entity 1 (A, B), FASTA

>7CVT_1 H(+)/Cl(-) exchange transporter ClcA (chains A, B)
MKTDTPSLETPQAARLRRRQLIRQLLERDKTPLAILFMAAVVGTLVGLAAVAFDKGVAWL
QNQRMGALVHTADNYPLLLTVAFLASAVLAMFGYFLVRKYAPEAGGSGIPEIEGALEDQR
PVRWWRVLPVKFFGGLGTLGGGMVLGREGPTVQIGGNIGRMVLDIFRLKGDEARHTLLAT
GAAAGLAAAFNAPAAGILFIIEEMRPQFRYTLISIKAVFIGVIMSTIMYRIFNCEVALID
VGKLSDAPLNTLWLYLILGIIFGIFGPIFNKWVLGMQDLLHRVHGGNITKWVLMGGAIGG
LCGLLGFVAPATSGGGFNLIPIATAGNFSMGMLVFIFVARVITTLLCFSSGAPGGIFAPM
LALGTVLGTAFGMVAVELFPQYHLEAGTFAIAGMGALLAASIRAPLTGIILVLEMTDNYQ
LILPMIITGLGATLLAQFTGGKPLYSAILARTLAKQEAEQLARSKAASASENT

Sequence of entity 2 (C, E), FASTA

>7CVT_2 antibody Fab fragment heavy chain (chains C, E)
EVRLLESGGGLVQPGGSLKLSCAASGFDYSRYWMSWVRQAPGKGLKWIGEINPVSSTINY
TPSLKDKFIISRDNAKDTLYLQISKVRSEDTALYYCARLYYGYGYWYFDVWGAGTTVTVS
SAKTTPPSVYPLAPGSAAAAASMVTLGCLVKGYFPEPVTVTWNSGSLAAGVHTFPAVLQA
ALYTLSSSVTVPSSSWPSETVTCNVAHPASSTKVDKKIVPRA

Sequence of entity 3 (D, F), FASTA

>7CVT_3 antibody Fab fragment light chain (chains D, F)
DIVLTQSPAIMSAAPGDKVTMTCSASSSVSYIHWYQQKSGTSPKRWIYDTSKLTSGVPVR
FSGSGSGTSYSLTINTMEAEDAATYYCQQWSSHPQTFGGGTKLEILRADAAPTVSIFPPS
SEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTL
TKDEYERHNSYTCEATHKTSTSPIVKSFNRA

Primary citation

Altering CLC stoichiometry by reducing non-polar side-chains at the dimerization interface. Mersch, K., Ozturk, T.N., Park, K. et al. J Mol Biol (2021) 433:166886-166886. DOI 10.1016/j.jmb.2021.166886 · 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
8GA1 2.6 Å, CLC-ec1 R230C/L249C/C85A at pH 4.5 100mM Cl Swap
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
8GAH 2.9 Å, CLC-ec1 L25C/A450C/C85A at pH 4.5 100mM Cl Twist

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