4P6I: Cas1-Cas2 complex from Escherichia coli

Crystal structure of the Cas1-Cas2 complex from Escherichia coli. Determined by X-ray diffraction at 2.3 Å resolution. Released 7 May 2014.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Escherichia coli
Chains: 6
Atoms: 10,450
Mol. weight: 156.05 kDa
Released: 7 May 2014

Explore 4P6I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4P6I contains 68 α-helices and 47 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: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2-9	8	1
α-helix	13-22	10
β-strand	24-27	4	1
β-strand	30-35	6	1
α-helix	37-50	14
β-strand	55-61	7	1
β-strand	68-74	7	1
α-helix	77-78	2
β-strand	79-83	5	2
β-strand	86-91	6	2
α-helix	92-94	3
α-helix	95-97	3

Chain B: 2 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2-9	8	3
α-helix	13-22	10
β-strand	24-27	4	3
β-strand	30-35	6	3
α-helix	37-50	14
β-strand	55-61	7	3
β-strand	68-73	6	3
β-strand	79-83	5	4
β-strand	86-91	6	4

Chain C: 15 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	17-20	4	5
β-strand	24-28	5	4
β-strand	31-35	5	4
β-strand	41-43	3	4
α-helix	46-48	3
β-strand	51-54	4	5
β-strand	59-60	2	4
α-helix	62-70	9
α-helix	73	1
β-strand	74-78	5	5
α-helix	80-82	3
β-strand	85-89	5	5
α-helix	96-107	12
α-helix	109-124	16
α-helix	134-156	23
α-helix	170-172	3
α-helix	175-197	23
α-helix	214-223	10
α-helix	228-237	10
α-helix	243-257	15
α-helix	260-272	13
α-helix	273-275	3
α-helix	277-280	4

Chain D: 15 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	8-10	3
α-helix	11-13	3
β-strand	15-20	6	5
β-strand	23-27	5	4
β-strand	32-35	4	4
β-strand	41-43	3	4
α-helix	46-48	3
β-strand	49-54	6	5
β-strand	58-61	4	4
α-helix	62-70	9
β-strand	74-78	5	5
β-strand	84-89	6	5
α-helix	96-107	12
α-helix	109-124	16
α-helix	127-129	3
α-helix	134-155	22
α-helix	176-198	23
α-helix	214-227	14
α-helix	229-238	10
α-helix	243-258	16
α-helix	260-273	14
α-helix	277-283	7
α-helix	287-294	8
β-strand	295	1	2

Chain E: 15 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	17-20	4	6
β-strand	23-28	6	2
β-strand	31-36	6	2
β-strand	41-44	4	2
β-strand	51-54	4	6
α-helix	55	1
β-strand	58-61	4	2
α-helix	62-71	10
α-helix	73	1
β-strand	74-78	5	6
α-helix	80-82	3
β-strand	85-89	5	6
α-helix	96-107	12
α-helix	109-123	15
α-helix	127-129	3
α-helix	134-156	23
α-helix	175-197	23
α-helix	214-223	10
α-helix	228-238	11
α-helix	243-257	15
α-helix	261-263	3
α-helix	264-272	9
α-helix	278-279	2

Chain F: 16 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	8-10	3
α-helix	11-13	3
β-strand	15-20	6	6
β-strand	23-28	6	2
β-strand	31-35	5	2
β-strand	41-43	3	2
α-helix	46-48	3
β-strand	49-54	6	6
β-strand	58-61	4	2
α-helix	62-70	9
β-strand	74-78	5	6
α-helix	80-82	3
β-strand	84-89	6	6
α-helix	96-107	12
α-helix	109-124	16
α-helix	127-129	3
α-helix	134-156	23
α-helix	175-198	24
α-helix	214-223	10
α-helix	224-228	5
α-helix	229-238	10
α-helix	243-258	16
α-helix	260-273	14
α-helix	277-282	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
CRISPR-associated endoribonuclease Cas2	A, B	protein	103	Escherichia coli	P45956 (AlphaFold model)
CRISPR-associated endonuclease Cas1	C, D, E, F	protein	305	Escherichia coli	Q46896 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4P6I_1 CRISPR-associated endoribonuclease Cas2 (chains A, B)
MSMLVVVTENVPPRLRGRLAIWLLEVRAGVYVGDVSAKIREMIWEQIAGLAEEGNVVMAW
ATNTETGFEFQTFGLNRRTPVDLDGLRLVSFLPVGSSENLYFQ

Sequence of entity 2 (C, D, E, F), FASTA

>4P6I_2 CRISPR-associated endonuclease Cas1 (chains C, D, E, F)
MTWLPLNPIPLKDRVSMIFLQYGQIDVIDGAFVLIDKTGIRTHIPVGSVACIMLEPGTRV
SHAAVRLAAQVGTLLVWVGEAGVRVYASGQPGGARSDKLLYQAKLALDEDLRLKVVRKMF
ELRFGEPAPARRSVEQLRGIEGSRVRATYALLAKQYGVTWNGRRYDPKDWEKGDTINQCI
SAATSCLYGVTEAAILAAGYAPAIGFVHTGKPLSFVYDIADIIKFDTVVPKAFEIARRNP
GEPDREVRLACRDIFRSSKTLAKLIPLIEDVLAAGEIQPPAPPEDAQPVAIPLPVSLGDA
GHRSS

Primary citation

Cas1-Cas2 complex formation mediates spacer acquisition during CRISPR-Cas adaptive immunity. Nunez, J.K., Kranzusch, P.J., Noeske, J. et al. Nat Struct Mol Biol (2014) 21:528-534. DOI 10.1038/nsmb.2820 · PubMed

Other PDB entries of the same protein (UniProt P45956 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4MAK 1.1 Å, Crystal structure of a putative ssRNA endonuclease Cas2, CRISPR adaptation protein from…
5DLJ 2.6 Å, Crystal Structure of Cas-DNA-N1 complex
4QDL 2.7 Å, Crystal structure of E.coli Cas1-Cas2 complex
5DQZ 2.7 Å, Crystal Structure of Cas-DNA-PAM complex
5VVK 2.9 Å, Cas1-Cas2 bound to full-site mimic
5DS5 2.95 Å, Crystal structure the Escherichia coli Cas1-Cas2 complex bound to protospacer DNA and Mg
5DQT 3.1 Å, Crystal Structure of Cas-DNA-22 complex
5DS4 3.2 Å, Crystal structure the Escherichia coli Cas1-Cas2 complex bound to protospacer DNA
5VVL 3.31 Å, Cas1-Cas2 bound to full-site mimic with Ni
5DS6 3.35 Å, Crystal structure the Escherichia coli Cas1-Cas2 complex bound to protospacer DNA with…
5WFE 3.64 Å, Cas1-Cas2-IHF-DNA holo-complex
5VVJ 3.89 Å, Cas1-Cas2 bound to half-site intermediate

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