2OL7: OspA mutant

The crystal structure of OspA mutant. Determined by X-ray diffraction at 1.35 Å resolution. Released 11 Dec 2007.

Method: X-ray diffraction
Resolution: 1.35 Å
Organism: Borrelia burgdorferi
Chains: 2
Atoms: 4,335
Mol. weight: 52.83 kDa
Released: 11 Dec 2007

Explore 2OL7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2OL7 contains 6 α-helices and 47 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: 3 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	29-33	5	1
β-strand	39-43	5	1
α-helix	51	1
β-strand	52-58	7	1
β-strand	61-67	7	1
β-strand	74-79	6	1
β-strand	85-90	6	1
β-strand	96-102	7	1
β-strand	109-117	9	1
β-strand	121-128	8	1
β-strand	131-139	9	1
β-strand	144-148	5	1
β-strand	156-161	6	1
β-strand	164	1	2
β-strand	166-171	6	1
β-strand	175-182	8	1
β-strand	185-192	8	1
β-strand	197-203	7	1
β-strand	212-217	6	3
β-strand	222-227	6	3
β-strand	230-237	8	3
β-strand	243-247	5	3
β-strand	248	1	4
α-helix	249	1
β-strand	255	1	4
β-strand	260-261	2	3
α-helix	265-272	8

Chain B: 3 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	30-33	4	5
β-strand	39-42	4	5
α-helix	51	1
β-strand	52-58	7	5
β-strand	61-67	7	5
β-strand	74-79	6	5
β-strand	85-90	6	5
β-strand	96-102	7	5
β-strand	109-117	9	5
β-strand	122-128	7	5
β-strand	131-138	8	5
β-strand	144-148	5	5
β-strand	156-161	6	5
β-strand	166-171	6	5
β-strand	176-182	7	5
β-strand	185-191	7	5
β-strand	197-203	7	5
β-strand	212-217	6	2
β-strand	222-227	6	2
β-strand	230-237	8	2
β-strand	243-247	5	2
β-strand	248	1	6
α-helix	249	1
β-strand	255	1	6
β-strand	260-261	2	2
α-helix	265-271	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Outer surface protein A	A, B	protein	251	Borrelia burgdorferi	P0CL66 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2OL7_1 Outer surface protein A (chains A, B)
GSHMKNSVSVDLPGSMKVLVSKSSNADGKYDLIATVDALELSGTSDKNNGSGVLEGVKAD
ASKVKLTISDDLGQTTLEVFKSDGSTLVSKKVTSKDKSSTEEKIIIDGIIIEKIITRADG
TRLEYTGIKSDGSGKAKEVLKGYVLEGTLTAEKTTLVVKEGTVTLSKNISKSGEVSVELN
DTDSSAATKKTAAWNSGTSTLTITVNSKKTKDLVFTSSNTITVQQYDSNGTSLEGSAVEI
TKLDEIKNALK

Primary citation

beta-Strand Flipping and Slipping Triggered by Turn Replacement Reveal the Opportunistic Nature of beta-Strand Pairing. Makabe, K., Yan, S., Tereshko, V. et al. J Am Chem Soc (2007) 129:14661-14669. DOI 10.1021/ja074252c · PubMed

Other PDB entries of the same protein (UniProt P0CL66 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2I5V 1.1 Å, Crystal structure of OspA mutant
2G8C 1.15 Å, Atomic-resolution crystal structure of Borrelia burgdorferi OspA via surface entropy…
2I5Z 1.2 Å, The crystal structure of OspA mutant
6J48 1.2 Å, Glycine mutation on single layer beta-sheet of OspAsm1
9WVV 1.27 Å, The crystal structure of OspA mutant
2OYB 1.3 Å, The crystal structure of OspA mutant
6KWV 1.37 Å, A Crystal Structure of OspA mutant
2PI3 1.4 Å, The crystal structure of OspA mutant
6ICS 1.4 Å, Loop deletion mutant (deleting four residues)
6KT1 1.43 Å, Crystal structure of an OspA mutant
6KWU 1.43 Å, A Crystal Structure of OspA mutant
6J6E 1.5 Å, Borrelia burgdorferi OspA via surface entropy reduction (form5)

Browse structure collections

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