2HCJ: Trypsin-modified Elongation Factor Tu

Trypsin-modified Elongation Factor Tu in complex with tetracycline. Determined by X-ray diffraction at 2.12 Å resolution. Released 31 Oct 2006.

Method: X-ray diffraction
Resolution: 2.12 Å
Organism: Escherichia coli
Chains: 2
Atoms: 3,143
Mol. weight: 41.9 kDa
Ligands: GDP, TAC, GLV, MG
Released: 31 Oct 2006

Explore 2HCJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2HCJ contains 15 α-helices and 28 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: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	9-10	2
β-strand	11-17	7	1
α-helix	24-39	16

Chain B: 13 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	65-70	6	1
β-strand	75-80	6	1
α-helix	84-93	10
β-strand	100-106	7	1
α-helix	113-124	12
β-strand	130-135	6	1
α-helix	143-159	17
α-helix	164-166	3
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	217-220	4	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	288	1	5
β-strand	290	1	5
β-strand	291-293	3	2
β-strand	300-310	11	6
α-helix	311-312	2
α-helix	313-315	3
β-strand	322-323	2	7
β-strand	329-332	4	6
β-strand	335-342	8	6
α-helix	343-344	2
β-strand	349-350	2	7
β-strand	355-367	13	6
β-strand	373-378	6	6
β-strand	381-391	11	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein chain elongation factor EF-Tu	A	protein	37	Escherichia coli	P0CE47 (AlphaFold model)
Protein chain elongation factor EF-Tu	B	protein	335	Escherichia coli	Q1R5Y2 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2HCJ_1 Protein chain elongation factor EF-Tu (chains A)
TKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAAR

Sequence of entity 2 (B), FASTA

>2HCJ_2 Protein chain elongation factor EF-Tu (chains B)
GITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREH
ILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKAL
EGDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKV
GEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTI
KPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKM
VVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLG

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	1
TAC	Tetracycline	C22 H24 N2 O8	1
GLV	Glyoxylic acid	C2 H2 O3	1
MG	Magnesium ion	Mg	1

Water and common crystallization additives (NA, SO4) are not listed.

Primary citation

Molecular complementarity between tetracycline and the GTPase active site of elongation factor Tu. Heffron, S.E., Mui, S., Aorora, A. et al. Acta Crystallogr D Biol Crystallogr (2006) 62:1392-1400. DOI 10.1107/S0907444906035426 · 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
4PC3 1.83 Å, Elongation factor Tu:Ts complex with partially bound GDP
5JBQ 2.01 Å, Ef-tu (escherichia coli) in complex with thiomuracin analog
1EFC 2.05 Å, Intact elongation factor from e.coli
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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