7MRX: Cryogenic crystal structure of barnase A43C/S80C

Cryogenic crystal structure of barnase A43C/S80C bound to barstar C40A/C82A. Determined by X-ray diffraction at 2.29 Å resolution. Released 18 May 2022.

Method: X-ray diffraction
Resolution: 2.29 Å
Organism: Bacillus amyloliquefaciens
Chains: 6
Atoms: 5,114
Mol. weight: 74.3 kDa
Released: 18 May 2022

Explore 7MRX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7MRX contains 30 α-helices and 30 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
α-helix	7-17	11
β-strand	24-25	2	1
α-helix	27-32	6
α-helix	37-39	3
α-helix	42-45	4
β-strand	50-51	2	1
β-strand	52-56	5	2
α-helix	64-65	2
β-strand	71-75	5	2
β-strand	87-91	5	2
β-strand	96-99	4	2
β-strand	107-108	2	2

Chain B: 5 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	1-6	6	3
α-helix	7-9	3
α-helix	13-23	11
α-helix	34-43	10
β-strand	49-54	6	3
α-helix	56-62	7
α-helix	66-79	14
β-strand	84-88	5	3

Chain C: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	7-17	11
β-strand	24-25	2	4
α-helix	27-32	6
α-helix	37-39	3
α-helix	42-45	4
β-strand	50-51	2	4
β-strand	52-55	4	5
α-helix	64-65	2
β-strand	71-75	5	5
β-strand	87-91	5	5
β-strand	96-99	4	5
β-strand	107-108	2	5

Chain D: 5 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	1-6	6	6
α-helix	7-9	3
α-helix	13-23	11
α-helix	34-43	10
β-strand	49-54	6	6
α-helix	56-61	6
α-helix	66-79	14
β-strand	84-88	5	6

Chain E: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	7-17	11
β-strand	24-25	2	7
α-helix	27-31	5
α-helix	37-39	3
α-helix	42-45	4
β-strand	50-51	2	7
β-strand	52-56	5	8
α-helix	64-65	2
β-strand	71-75	5	8
β-strand	87-91	5	8
β-strand	96-99	4	8
β-strand	107-108	2	8

Chain F: 5 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	9
α-helix	7-9	3
α-helix	13-23	11
α-helix	34-43	10
β-strand	49-54	6	9
α-helix	56-62	7
α-helix	66-79	14
β-strand	84-88	5	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ribonuclease	A, C, E	protein	128	Bacillus amyloliquefaciens	P00648 (AlphaFold model)
Barstar	B, D, F	protein	90	Bacillus amyloliquefaciens	P11540 (AlphaFold model)

Sequence of entity 1 (A, C, E), FASTA

>7MRX_1 Ribonuclease (chains A, C, E)
MGSSHHHHHHSQAPIEGRAQVINTFDGVADYLQTYHKLPDNYITKSEAQALGWVASKGNL
CDVAPGKSIGGDIFSNREGKLPGKSGRTWREADINYTCGFRNSDRILYSSDWLIYKTTDH
YQTFTKIR

Sequence of entity 2 (B, D, F), FASTA

>7MRX_2 Barstar (chains B, D, F)
MKKAVINGEQIRSISDLHQTLKKELALPEYYGENLDALWDALTGWVEYPLVLEWRQFEQS
KQLTENGAESVLQVFREAKAEGADITIILS

Primary citation

Conformational entropy and protein affinity. Caro, J.A., Wand, A.J. To be published.

Other PDB entries of the same protein (UniProt P00648 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6PQK 1.2 Å, Cryogenic crystal structure of barnase A43C/S80C bound to barstar C40A/S59C/A67C/C82A
2C4B 1.3 Å, Inhibitor cystine knot protein McoEeTI fused to the catalytically inactive barnase…
1A2P 1.5 Å, Barnase wildtype structure at 1.5 Å resolution
2ZA4 1.58 Å, Crystal Structural Analysis of Barnase-barstar Complex
1B20 1.7 Å, Deletion of a buried salt-bridge in barnase
1BRN 1.76 Å, Subsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76 Å…
1B2X 1.8 Å, Barnase wildtype structure at PH 7.5 from a cryo_cooled crystal at 100K
1B2S 1.82 Å, Structural response to mutation at a protein-protein interface
1BRI 1.9 Å, Barnase mutant with ile 76 replaced by ala
1RNB 1.9 Å, Crystal structure of a barnase-d(*gp*c) complex at 1.9 Å resolution
1X1Y 1.9 Å, Water-mediate interaction at aprotein-protein interface
3KCH 1.94 Å, Baranase crosslinked by glutaraldehyde

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