PDBsum entry 1f1m

Immune system

PDB id: 1f1m

Contents

Protein chains

162 a.a. *

Metals

_ZN ×6

Waters ×632

* Residue conservation analysis

PDB id:

1f1m

Name:

Immune system

Title:

Crystal structure of outer surface protein c (ospc)

Structure:

Outer surface protein c. Chain: a, b, c, d. Fragment: residues 38-201. Synonym: ospc. Engineered: yes. Mutation: yes

Source:

Borrelia burgdorferi. Lyme disease spirochete. Organism_taxid: 139. Strain: hb19. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Dimer (from PQS)

Resolution:

1.80Å R-factor: 0.201 R-free: 0.235

Authors:

D.Kumaran,S.Eswaramoorthy,J.J.Dunn,S.Swaminathan

Key ref:

D.Kumaran et al. (2001). Crystal structure of outer surface protein C (OspC) from the Lyme disease spirochete, Borrelia burgdorferi. EMBO J, 20, 971-978. PubMed id: 11230121 DOI: 10.1093/emboj/20.5.971

Date:

19-May-00 Release date: 04-Apr-01

Protein chains

Q9AGB1  (Q9AGB1_BORBG) -  OspC-modified from Borreliella burgdorferi

Seq: 165 a.a.

Struc: 162 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1093/emboj/20.5.971

EMBO J 20:971-978 (2001)

PubMed id: 11230121

Crystal structure of outer surface protein C (OspC) from the Lyme disease spirochete, Borrelia burgdorferi.

D.Kumaran, S.Eswaramoorthy, B.J.Luft, S.Koide, J.J.Dunn, C.L.Lawson, S.Swaminathan.

ABSTRACT

Outer surface protein C (OspC) is a major antigen on the surface of the Lyme disease spirochete, Borrelia burgdorferi, when it is being transmitted to humans. Crystal structures of OspC have been determined for strains HB19 and B31 to 1.8 and 2.5 A resolution, respectively. The three-dimensional structure is predominantly helical. This is in contrast to the structure of OspA, a major surface protein mainly present when spirochetes are residing in the midgut of unfed ticks, which is mostly beta-sheet. The surface of OspC that would project away from the spirochete's membrane has a region of strong negative electrostatic potential which may be involved in binding to positively charged host ligands. This feature is present only on OspCs from strains known to cause invasive human disease.

Selected figure(s)

Figure 1.
Figure 1 (A) RIBBONS (Carson, 1991) representation of the OspC-HB19 dimer. The two monomers are colored red and green, respectively. The close proximity of the two inner most helices indicates that it is a tight dimer. (B) Topology diagram of the OspC-HB19 monomer. Red cylinders represent -helices and green arrows -strands. (C) The dimeric interface. Residues interacting across the 2-fold axis are shown as a ball-and-stick model. For clarity only 1 and 1' helices are shown. (D) Superposition of Borrelia OspC-HB19 (green) and Salmonella AR (magenta) monomers. The r.m.s.d. between 122 aligned C atoms is 3.0 Å. Alignment was carried out with SCOP (Murzin et al., 1995).

Figure 2.
Figure 2 Stereo view of putative binding site and cavities. The cavities as calculated by GRASP (Nicholls et al., 1991) are shown in different colors. Cavities shown in blue and green are at the top of the molecule away from the membrane surface. Residues forming these cavities are shown as a stick model in corresponding colors. Each cavity has a volume of 50 Å3 and is formed by residues Ala75, Ile76, Gly77, Lys78, Lys79, Glu89, Ala90, Asp91, His92 and Asn93 of one monomer, and Gly94, Ser95, Ser98, Gly146, Lys147 and Glu148 of the other monomer. The solvent structures in the cavities are remarkably well conserved between the HB19 and B31 molecules.

The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2001, 20, 971-978) copyright 2001.

Figures were selected by the author.