4PC3: Elongation factor Tu 1

Elongation factor Tu:Ts complex with partially bound GDP. Determined by X-ray diffraction at 1.83 Å resolution. Released 6 May 2015.

Method: X-ray diffraction
Resolution: 1.83 Å
Organism: Escherichia coli
Chains: 4
Atoms: 11,293
Mol. weight: 148.69 kDa
Ligands: GDP
Released: 6 May 2015

Explore 4PC3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4PC3 contains 53 α-helices and 74 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: 14 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	11-18	8	1
α-helix	24-39	16
β-strand	66-70	5	1
β-strand	75-80	6	1
α-helix	84-93	10
α-helix	95-98	4
β-strand	100-106	7	1
α-helix	115-124	10
β-strand	130-135	6	1
α-helix	137-139	3
α-helix	143-159	17
β-strand	169-171	3	1
α-helix	174-178	5
α-helix	182-198	17
α-helix	200-204	5
α-helix	205-207	3
α-helix	209-210	2
β-strand	211-213	3	2
β-strand	216-220	5	3
β-strand	224-230	7	3
β-strand	233	1	2
β-strand	235-237	3	4
β-strand	241-246	6	2
β-strand	248-254	7	2
β-strand	255-260	6	3
β-strand	263-265	3	3
β-strand	267-269	3	4
β-strand	273-278	6	3
α-helix	283-285	3
β-strand	291-293	3	2
β-strand	300-310	11	5
α-helix	311-312	2
β-strand	322	1	6
β-strand	329-332	4	5
β-strand	335-342	8	5
α-helix	343-344	2
β-strand	350	1	6
β-strand	355-367	13	5
β-strand	373-378	6	5
β-strand	381-391	11	5

Chain B: 13 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	11-18	8	11
α-helix	24-39	16
β-strand	67-70	4	11
β-strand	75-80	6	11
α-helix	84-93	10
β-strand	100-106	7	11
α-helix	115-124	10
β-strand	130-135	6	11
α-helix	137-139	3
α-helix	143-159	17
β-strand	169-171	3	11
α-helix	174-178	5
α-helix	182-198	17
α-helix	200-204	5
α-helix	205-207	3
α-helix	209-210	2
β-strand	211-213	3	12
β-strand	217-220	4	13
β-strand	224-230	7	13
β-strand	233	1	12
β-strand	235-237	3	14
β-strand	241-246	6	12
β-strand	248-254	7	12
β-strand	255-260	6	13
β-strand	263-265	3	13
β-strand	267-269	3	14
β-strand	273-278	6	13
α-helix	283-285	3
β-strand	288	1	15
β-strand	290	1	15
β-strand	291-293	3	12
β-strand	300-310	11	16
α-helix	311-312	2
β-strand	322	1	17
β-strand	329-332	4	16
β-strand	335-342	8	16
α-helix	343-344	2
β-strand	350	1	17
β-strand	355-367	13	16
β-strand	373-378	6	16
β-strand	381-391	11	16

Chain C: 13 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	5-15	11
α-helix	19-28	10
α-helix	33-51	19
β-strand	58-66	9	7
β-strand	69-77	9	7
α-helix	80-84	5
α-helix	86-102	17
α-helix	107-125	19
β-strand	130-138	9	7
β-strand	141-147	7	8
β-strand	151-158	8	8
α-helix	162-175	14
β-strand	179	1	9
α-helix	182-184	3
α-helix	187-203	17
α-helix	208-225	18
β-strand	227	1	9
β-strand	232	1	10
α-helix	233	1
β-strand	240	1	10
α-helix	241-247	7
β-strand	251-259	9	8
α-helix	271-278	8

Chain D: 13 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	5-15	11
α-helix	19-28	10
α-helix	33-51	19
β-strand	58-66	9	18
β-strand	69-77	9	18
α-helix	80-83	4
α-helix	86-102	17
α-helix	107-125	19
β-strand	130-138	9	18
β-strand	141-147	7	19
β-strand	151-158	8	19
α-helix	162-175	14
β-strand	179	1	20
α-helix	182-184	3
α-helix	187-203	17
α-helix	208-226	19
β-strand	227	1	20
β-strand	232-233	2	21
β-strand	236-240	5	21
α-helix	241-247	7
β-strand	251-259	9	19
α-helix	265-268	4
α-helix	271-278	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Elongation factor Tu 1	A, B	protein	394	Escherichia coli	P0CE47 (AlphaFold model)
Elongation factor Ts	C, D	protein	282	Escherichia coli	P0A6P1 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4PC3_1 Elongation factor Tu 1 (chains A, B)
MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARG
ITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHI
LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALE
GDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVG
EEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIK
PHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMV
VTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLG

Sequence of entity 2 (C, D), FASTA

>4PC3_2 Elongation factor Ts (chains C, D)
AEITASLVKELRERTGAGMMDCKKALTEANGDIELAIENMRKSGAIKAAKKAGNVAADGV
IKTKIDGNYGIILEVNCQTDFVAKDAGFQAFADKVLDAAVAGKITDVEVLKAQFEEERVA
LVAKIGENINIRRVAALEGDVLGSYQHGARIGVLVAAKGADEELVKHIAMHVAASKPEFI
KPEDVSAEVVEKEYQVQLDIAMQSGKPKEIAEKMVEGRMKKFTGEVSLTGQPFVMEPSKT
VGQLLKEHNAEVTGFIRFEVGEGIEKVETDFAAEVAAMSKQS

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	2

Water and common crystallization additives (GOL) are not listed.

Primary citation

Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu. Thirup, S.S., Van, L.B., Nielsen, T.K. et al. J Struct Biol (2015) 191:10-21. DOI 10.1016/j.jsb.2015.06.011 · PubMed

Other PDB entries of the same protein (UniProt P0CE47 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9TBU 1.23 Å, E. coli EF-Tu-T62A:GDP AMPylated at T65
5JBQ 2.01 Å, Ef-tu (escherichia coli) in complex with thiomuracin analog
1EFC 2.05 Å, Intact elongation factor from e.coli
2HCJ 2.12 Å, Trypsin-modified Elongation Factor Tu in complex with tetracycline
3U6B 2.12 Å, Ef-tu (escherichia coli) in complex with nvp-ldi028
4P3Y 2.15 Å, Crystal structure of Acinetobacter baumannii DsbA in complex with EF-Tu
5MI8 2.18 Å, Structure of the phosphomimetic mutant of EF-Tu T383E
8FR3 2.23 Å, E. coli EF-Tu in complex with KKL-55
4G5G 2.3 Å, ef-tu (Escherichia coli) complexed with nvp-ldu796
1D8T 2.35 Å, Crystal structure of elongation factor, tu (ef-tu-mggdp) complexed with GE2270A, a…
5I4Q 2.35 Å, Contact-dependent inhibition system from Escherichia coli NC101 - ternary…
3U6K 2.45 Å, Ef-tu (escherichia coli) in complex with nvp-ldk733

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