6KEA: MBP-tagged REV7-IpaB complex

crystal structure of MBP-tagged REV7-IpaB complex. Determined by X-ray diffraction at 2.35 Å resolution. Released 11 Sept 2019.

Method: X-ray diffraction
Resolution: 2.35 Å
Organisms: Escherichia coli (strain K12), synthetic construct, Homo sapiens
Chains: 4
Atoms: 18,392
Mol. weight: 275.85 kDa
Released: 11 Sept 2019

Explore 6KEA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6KEA contains 134 α-helices and 130 β-strands across 4 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: 35 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	7-11	5	1
α-helix	18-32	15
β-strand	35-39	5	1
α-helix	44-51	8
β-strand	60-64	5	1
α-helix	65-67	3
α-helix	68-73	6
β-strand	77	1	2
α-helix	84-87	4
β-strand	90	1	3
α-helix	92-95	4
β-strand	99-100	2	4
β-strand	103-104	2	4
β-strand	107-112	6	1
β-strand	115-119	5	5
β-strand	129	1	6
α-helix	130-132	3
α-helix	133-141	9
β-strand	146-148	3	5
α-helix	155-162	8
α-helix	163-165	3
β-strand	168-173	6	7
β-strand	176-183	8	7
α-helix	187-201	15
α-helix	211-219	9
β-strand	223-228	6	5
α-helix	230-232	3
α-helix	233-237	5
β-strand	243-246	4	5
α-helix	247-249	3
β-strand	250-251	2	6
β-strand	254-255	2	6
β-strand	259-260	2	8
β-strand	261-267	7	1
β-strand	268	1	2
α-helix	274-279	6
α-helix	280-285	6
α-helix	288-297	10
β-strand	302-303	2	1
β-strand	305	1	3
α-helix	306-312	7
α-helix	316-326	11
β-strand	329-330	2	8
α-helix	331-332	2
α-helix	337-352	16
α-helix	358-369	12
α-helix	371-394	24
α-helix	400-402	3
β-strand	403-408	6	9
β-strand	411-416	6	9
α-helix	419-437	19
β-strand	441-449	9	10
β-strand	455-464	10	10
α-helix	469	1
α-helix	471	1
α-helix	476-492	17
α-helix	494-497	4
α-helix	499-502	4
β-strand	506-513	8	10
α-helix	520-523	4
β-strand	532-534	3	10
α-helix	535-536	2
α-helix	537-540	4
β-strand	545-554	10	10
β-strand	559-567	9	10
β-strand	609-612	4	10
α-helix	615-618	4

Chain B: 32 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	7-11	5	11
α-helix	18-32	15
β-strand	35-39	5	11
α-helix	44-52	9
β-strand	60-64	5	11
α-helix	65-67	3
α-helix	68-73	6
β-strand	77	1	12
α-helix	78-80	3
α-helix	84-87	4
β-strand	90	1	13
α-helix	92-98	7
β-strand	99-100	2	14
β-strand	103-104	2	14
β-strand	107-112	6	11
β-strand	115-119	5	15
β-strand	129	1	16
α-helix	130-132	3
α-helix	133-142	10
β-strand	146-148	3	15
α-helix	155-163	9
β-strand	168-173	6	17
β-strand	176-183	8	17
α-helix	187-201	15
α-helix	211-219	9
β-strand	223-228	6	15
α-helix	230-232	3
β-strand	243-246	4	15
α-helix	247-249	3
β-strand	250-251	2	16
β-strand	254-255	2	16
α-helix	256	1
β-strand	259-260	2	18
β-strand	261-267	7	11
β-strand	268	1	12
α-helix	274-279	6
α-helix	280-285	6
α-helix	288-297	10
β-strand	302-303	2	11
β-strand	305	1	13
α-helix	306-312	7
α-helix	316-326	11
β-strand	329-330	2	18
α-helix	331-332	2
α-helix	337-353	17
α-helix	358-369	12
α-helix	371-394	24
α-helix	400-402	3
β-strand	403-408	6	19
β-strand	411-416	6	19
α-helix	419-437	19
β-strand	441-449	9	20
β-strand	455-464	10	20
α-helix	474-492	19
α-helix	494-496	3
α-helix	499-502	4
β-strand	506-513	8	20
β-strand	532-534	3	20
α-helix	535-536	2
α-helix	537-540	4
β-strand	546-553	8	20
β-strand	559-566	8	20
β-strand	609-612	4	20
α-helix	616-618	3

Chain C: 33 helices, 33 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	21
α-helix	18-32	15
β-strand	36-39	4	21
α-helix	44-53	10
β-strand	60-64	5	21
α-helix	65-73	9
β-strand	77	1	22
α-helix	78-80	3
α-helix	84-87	4
β-strand	90	1	23
α-helix	92-97	6
β-strand	99-100	2	24
β-strand	103-104	2	24
β-strand	107-112	6	21
β-strand	115-119	5	25
β-strand	129	1	26
α-helix	130-132	3
α-helix	133-141	9
β-strand	146-148	3	25
α-helix	155-164	10
β-strand	168-173	6	27
β-strand	176-183	8	27
α-helix	187-201	15
α-helix	211-219	9
β-strand	223-228	6	25
α-helix	230-232	3
α-helix	233-238	6
β-strand	243-246	4	25
α-helix	247-249	3
β-strand	250	1	26
β-strand	251	1	28
β-strand	254	1	28
α-helix	255-256	2
β-strand	259-260	2	29
β-strand	261-267	7	21
β-strand	268	1	22
α-helix	274-279	6
α-helix	280-285	6
α-helix	288-297	10
β-strand	302-303	2	21
β-strand	305	1	23
α-helix	306-312	7
α-helix	316-326	11
β-strand	329-330	2	29
α-helix	331-332	2
α-helix	337-353	17
α-helix	358-369	12
α-helix	371-394	24
α-helix	400-402	3
β-strand	403-408	6	30
β-strand	411-416	6	30
α-helix	419-437	19
β-strand	441-449	9	31
β-strand	455-464	10	31
α-helix	476-492	17
α-helix	494-496	3
α-helix	499-502	4
β-strand	506-513	8	31
α-helix	517-523	7
β-strand	532-534	3	31
α-helix	535-536	2
α-helix	537-540	4
β-strand	546-554	9	31
β-strand	559-566	8	31
β-strand	609-612	4	31
α-helix	615-617	3

Chain D: 34 helices, 33 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	32
α-helix	18-32	15
β-strand	36-39	4	32
α-helix	48-52	5
β-strand	60-64	5	32
α-helix	65-67	3
α-helix	68-73	6
β-strand	77	1	33
α-helix	78-80	3
α-helix	84-87	4
β-strand	90	1	34
α-helix	92-95	4
β-strand	99-100	2	35
β-strand	103-104	2	35
β-strand	107-112	6	32
β-strand	115-119	5	36
β-strand	129	1	37
α-helix	130-132	3
α-helix	133-142	10
β-strand	146-148	3	36
α-helix	155-162	8
β-strand	168-173	6	38
β-strand	176-183	8	38
α-helix	187-201	15
α-helix	211-219	9
β-strand	223-228	6	36
α-helix	230-232	3
α-helix	233-236	4
β-strand	243-246	4	36
α-helix	247-249	3
β-strand	250	1	37
β-strand	251	1	39
β-strand	254	1	39
α-helix	255-256	2
β-strand	259-260	2	40
β-strand	261-267	7	32
β-strand	268	1	33
α-helix	274-279	6
α-helix	280-285	6
α-helix	288-297	10
β-strand	302-303	2	32
β-strand	305	1	34
α-helix	306-312	7
α-helix	316-326	11
β-strand	329-330	2	40
α-helix	331-332	2
α-helix	337-352	16
α-helix	358-369	12
α-helix	371-394	24
α-helix	400-402	3
β-strand	403-408	6	41
β-strand	411-416	6	41
α-helix	419-437	19
β-strand	441-449	9	42
β-strand	455-464	10	42
α-helix	472-473	2
α-helix	477-493	17
α-helix	494-496	3
α-helix	499-502	4
β-strand	506-513	8	42
α-helix	520-523	4
β-strand	532-534	3	42
α-helix	537-540	4
β-strand	546-553	8	42
β-strand	559-566	8	42
β-strand	609-612	4	42
α-helix	616-619	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Maltose-binding periplasmic protein,LINKER,hREV7,LINKER,Invasin IpaB,hREV3	A, B, C, D	protein	631	Escherichia coli (strain K12), synthetic construct, Homo sapiens, Shigella flexneri	O60673, P0AEX9 (AlphaFold model), P18011 (AlphaFold model), Q9UI95 (AlphaFold model)

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

>6KEA_1 Maltose-binding periplasmic protein,LINKER,hREV7,LINKER,Invasin IpaB,hREV3 (chains A, B, C, D)
MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI
IFWAHDRFGGYAQSGLLAEITPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK
DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYAAGKYDIK
DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA
VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL
GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDA
ALAAAQTNAAAAAQVVADVLCEFLEVAVHLILYVREVYPVGIFQKRKKYNVPVQMSCHPE
LNQYIQDTLHCVKPLLEKNDVEKVVVVILDKEHRPVEKFVFEITQPPLLSISSDSLLSHV
EQLLAAFILKISVCDAVLDHNPPGCTFTVLVHTREAATRNMEKIQVIKDFPWILADEQDV
HMHDPRLIPLKTMTSDILKMQLYVEERAHKGSASGSGSGSGSGSGSGSGSGSGSHMNINT
TNAHSTSNILIPELKAPKSLNASREEIMATL

Primary citation

REV7 has a dynamic adaptor region to accommodate small GTPase RAN/ShigellaIpaB ligands, and its activity is regulated by the RanGTP/GDP switch. Wang, X., Pernicone, N., Pertz, L. et al. J Biol Chem (2019) 294:15733-15742. DOI 10.1074/jbc.RA119.010123 · PubMed

Other PDB entries of the same protein (UniProt O60673), best resolution first:

6BCD 1.43 Å, Crystal structure of Rev7-K44A/R124A/A135D in complex with Rev3-RBM2 (residues 1988-2014)
6BC8 1.68 Å, Crystal structure of Rev7-R124A/Rev3-RBM2 (residues 1988-2014) complex
5O8K 1.8 Å, Crystal structure of mammalian Rev7 in complex with Rev3 1875-1895
3ABD 1.9 Å, Structure of human REV7 in complex with a human REV3 fragment in a monoclinic crystal
4EXT 1.9 Å, Structure of polymerase-interacting domain of human Rev1 in complex with translesional…
6WS0 2.24 Å, Rational drug design of phenazopyridine derivatives as novel inhibitors of Rev1-CT
6WS5 2.47 Å, Rational drug design of phenazopyridine derivatives as novel inhibitors of Rev1-CT
3ABE 2.6 Å, Structure of human REV7 in complex with a human REV3 fragment in a tetragonal crystal
4GK0 2.7 Å, Crystal structure of human Rev3-Rev7-Rev1 complex
6EKM 2.76 Å, Crystal structure of mammalian Rev7 in complex with human Rev3 second binding site
3VU7 2.8 Å, Crystal structure of REV1-REV7-REV3 ternary complex
6BI7 2.8 Å, Crystal structure of Rev7-WT/Rev3 as a monomer under high-salt conditions

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