4FME: EspG-Rab1-Arf6 complex

EspG-Rab1-Arf6 complex. Determined by X-ray diffraction at 4.1 Å resolution. Released 5 Sept 2012.

Method: X-ray diffraction
Resolution: 4.1 Å
Organisms: Escherichia coli, Homo sapiens
Chains: 6
Atoms: 10,910
Mol. weight: 155.88 kDa
Ligands: AF3, GDP, MG, GTP
Released: 5 Sept 2012

Explore 4FME in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4FME contains 60 α-helices and 70 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.

Chains A and D: 13 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	50-60	11
α-helix	70-79	10
β-strand	83-85	3	1
β-strand	91-98	8	1
β-strand	104-110	7	1
β-strand	115-119	5	1
β-strand	127-131	5	1
α-helix	139-141	3
β-strand	146-147	2	2
β-strand	151	1	3
β-strand	153-156	4	2
α-helix	166-176	11
β-strand	181-183	3	2
α-helix	204-207	4
β-strand	214-217	4	2
β-strand	220-222	3	2
α-helix	224-233	10
α-helix	245-250	6
α-helix	254-262	9
α-helix	268-277	10
α-helix	281-290	10
α-helix	294-296	3
α-helix	297-315	19
β-strand	325-332	8	2
β-strand	338-349	12	2
β-strand	358-368	11	2
α-helix	379-383	5
β-strand	387-394	8	2

Chain B: 10 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	10-16	7	4
α-helix	26-32	7
α-helix	41-43	3
β-strand	46-49	4	4
β-strand	53-54	2	4
β-strand	59-67	9	4
α-helix	71-73	3
α-helix	74-77	4
α-helix	78-80	3
β-strand	86-87	2	4
β-strand	90-92	3	5
α-helix	96-100	5
α-helix	102-112	11
β-strand	118-119	2	4
β-strand	122-124	3	5
α-helix	129-131	3
α-helix	136-146	11
β-strand	151-152	2	5
β-strand	154	1	6
β-strand	159	1	6
α-helix	163-171	9

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

Element	Residues	Length	Sheet
β-strand	15-19	5	7
α-helix	27-35	9
β-strand	41	1	3
β-strand	47-54	8	7
β-strand	57-64	8	7
α-helix	72-77	6
β-strand	83-89	7	7
α-helix	93-95	3
α-helix	96-108	13
α-helix	110-112	3
β-strand	116-122	7	7
α-helix	132-138	7
β-strand	149-153	5	7
β-strand	155	1	8
β-strand	160	1	8
α-helix	164-171	8

Chain E: 10 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	10-16	7	12
α-helix	24-32	9
α-helix	41-43	3
β-strand	46-49	4	12
β-strand	53-54	2	12
β-strand	59-67	9	12
α-helix	71-73	3
α-helix	74-77	4
α-helix	78-80	3
β-strand	86-87	2	12
β-strand	90-92	3	13
α-helix	96-100	5
α-helix	102-112	11
β-strand	118-119	2	12
β-strand	122-124	3	13
α-helix	129-131	3
α-helix	136-146	11
β-strand	151-152	2	13
β-strand	154	1	14
β-strand	159	1	14
α-helix	163-171	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
EspG protein	A, D	protein	351	Escherichia coli	Q7DB50 (AlphaFold model)
Ras-related protein Rab-1A	B, E	protein	171	Homo sapiens	P62820 (AlphaFold model)
ADP-ribosylation factor 6	C, F	protein	160	Homo sapiens	P62330 (AlphaFold model)

Sequence of entity 1 (A, D), FASTA

>4FME_1 EspG protein (chains A, D)
EMSCAEKLLKVLSFGLWNPTYSRSERQSFQELLTVLEPVYPLPNELGRVSARFSDGSSLR
ISVTNSESIEAEIRTPNNEKITVLLESNEQNRLLQSLPIDRHMPYIQVHRALSEMDLTDT
TSMRNLLGFTSKLSTTLIPHNAQTDPLSGPTPFSSIFMDTCRGLGNAKLSLNGVDIPANA
QMLLRDALGLKDTHSSPTRNVIDHGISRHDAEQIARESSGSDKQKAEVVEFLCHPEAATA
ICSAFYQSFNVPALTLTHERISKASEYNAERSLDTPNACINISISQSSDGNIYVTSHTGV
LIMAPEDRPNEMGMLTNRTSYEVPQGVKCTIDEMVRALQPRYAASETYLQN

Sequence of entity 2 (B, E), FASTA

>4FME_2 Ras-related protein Rab-1A (chains B, E)
PEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIW
DTAGQERFRTITSSYYRGAHGIIVVYDVTDQESFNNVKQWLQEIDRYASENVNKLLVGNK
CDLTTKKVVDYTTAKEFADSLGIPFLETSAKNATNVEQSFMTMAAEIKKRM

Sequence of entity 3 (C, F), FASTA

>4FME_3 ADP-ribosylation factor 6 (chains C, F)
MRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYKNVKFNVWDVGGQDKIRPL
WRHYYTGTQGLIFVVDCADRDRIDEARQELHRIINDREMRDAIILIFANKQDLPDAMKPH
EIQEKLGLTRIRDRNWYVQPSCATSGDGLYEGLTWLTSNY

Ligands and cofactors

ID	Name	Formula	Copies
AF3	Aluminum fluoride	Al F3	2
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	2
MG	Magnesium ion	Mg	4
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	2

Primary citation

Structurally Distinct Bacterial TBC-like GAPs Link Arf GTPase to Rab1 Inactivation to Counteract Host Defenses. Dong, N., Zhu, Y., Lu, Q. et al. Cell (2012) 150:1029-1041. DOI 10.1016/j.cell.2012.06.050 · PubMed

Other PDB entries of the same protein (UniProt Q7DB50 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3PCR 2.5 Å, Structure of EspG-Arf6 complex
4FMC 2.8 Å, EspG-Rab1 complex
3PCS 2.86 Å, Structure of EspG-PAK2 autoinhibitory Ialpha3 helix complex
4FMD 3.05 Å, EspG-Rab1 complex structure at 3.05 A

Browse structure collections

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