1JL2: Chimera of Ribonuclease HI, Ribonuclease H

Crystal structure of TCEO RNase H-a chimera combining the folding core from T. thermophilus RNase H and the remaining region of E. coli RNase H. Determined by X-ray diffraction at 1.76 Å resolution. Released 18 Jan 2002.

Method: X-ray diffraction
Resolution: 1.76 Å
Organisms: Escherichia coli (strain K12), Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Chains: 4
Atoms: 4,705
Mol. weight: 70.4 kDa
Released: 18 Jan 2002

Explore 1JL2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1JL2 contains 18 α-helices and 26 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: 6 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	4-13	10	1
β-strand	18-27	10	1
β-strand	32-42	11	1
α-helix	44-57	14
β-strand	64-69	6	1
α-helix	72-79	8
α-helix	82-88	7
β-strand	92	1	2
β-strand	98	1	2
α-helix	99	1
α-helix	102-112	11
β-strand	116-121	6	1
α-helix	129-142	14
β-strand	147	1	1

Chain B: 4 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	4-13	10	3
β-strand	18-28	11	3
β-strand	31-42	12	3
α-helix	44-57	14
β-strand	64-69	6	3
α-helix	72-79	8
α-helix	102-112	11
β-strand	116-121	6	3
α-helix	129-143	15
β-strand	147	1	3

Chain C: 4 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	4-13	10	4
β-strand	18-27	10	4
β-strand	32-42	11	4
α-helix	44-57	14
β-strand	64-69	6	4
α-helix	72-78	7
α-helix	102-112	11
β-strand	116-121	6	4
α-helix	129-142	14
β-strand	147	1	4

Chain D: 4 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	4-13	10	5
β-strand	18-28	11	5
β-strand	31-42	12	5
α-helix	44-57	14
β-strand	64-69	6	5
α-helix	72-79	8
α-helix	102-112	11
β-strand	116-121	6	5
α-helix	129-142	14
β-strand	147	1	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Chimera of Ribonuclease HI, Ribonuclease H	A, B, C, D	protein	156	Escherichia coli (strain K12), Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)	P0A7Y4 (AlphaFold model), P29253 (AlphaFold model)

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

>1JL2_1 Chimera of Ribonuclease HI, Ribonuclease H (chains A, B, C, D)
MLKQVEIFTDGSALGNPGPGGYGAILRYRGREKTFSAGYTRTTNNRMELKAAIEGLKALK
EPAEVDLYTDSHYLKKAFTEGWLEGWRKRGWRTAEGKPVKNRDLWEALLLAMAPHRVRFH
FVKGHAGHPENERADELARAAAMNPTLEDTGYQVEV

Primary citation

Contributions of folding cores to the thermostabilities of two ribonucleases H. Robic, S., Berger, J.M., Marqusee, S. Protein Sci (2002) 11:381-389. DOI 10.1110/ps.38602 · PubMed

Other PDB entries of the same protein (UniProt P0A7Y4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1JL1 1.3 Å, D10A E. coli ribonuclease HI
1F21 1.4 Å, Divalent metal cofactor binding in the kinetic folding trajectory of E. Coli…
2YV0 1.4 Å, Structural and Thermodynamic Analyses of E. coli ribonuclease HI Variant with Quintuple…
3QIO 1.4 Å, Crystal Structure of HIV-1 RNase H with engineered E. coli loop and N-hydroxy…
2RN2 1.48 Å, Structural details of ribonuclease H from escherichia coli as refined to an atomic…
1JXB 1.6 Å, I53A, a point mutant of the cysteine-free variant of E. coli Rnase HI
3QIN 1.7 Å, Crystal Structure of HIV-1 RNase H p15 with engineered E. coli loop and pyrimidinol…
3HYF 1.7 Å, Crystal structure of HIV-1 RNase H p15 with engineered E. coli loop and active site…
7VSD 1.7 Å, E. coli Ribonuclease HI in complex with one Mg2+ (2)
7VSA 1.76 Å, E. coli Ribonuclease HI in complex with two Mg2+
3AA4 1.79 Å, A52V E.coli RNase HI
1KVA 1.8 Å, E. Coli ribonuclease hi D134A mutant

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