PDBsum entry 2mlh

Membrane protein

PDB id: 2mlh

Contents

Protein chain

238 a.a.

PDB id:

2mlh

Name:

Membrane protein

Title:

Nmr solution structure of opa60 from n. Gonorrhoeae in fc-12 micelles

Structure:

Opacity protein opa60. Chain: a. Engineered: yes

Source:

Neisseria gonorrhoeae. Organism_taxid: 485. Strain: ms11. Gene: opah. Expressed in: neisseria gonorrhoeae. Expression_system_taxid: 485.

NMR struc:

20 models

Authors:

D.A.Fox,P.Larsson,R.H.Lo,B.M.Kroncke,P.M.Kasson,L.Columbus

Key ref:

D.A.Fox et al. (2014). Structure of the Neisserial outer membrane protein Opa₆₀: loop flexibility essential to receptor recognition and bacterial engulfment. J Am Chem Soc, 136, 9938-9946. PubMed id: 24813921 DOI: 10.1021/ja503093y

Date:

27-Feb-14 Release date: 25-Jun-14

Protein chain

Q04884  (OPAH_NEIGO) -  Opacity protein opA60 (Fragment) from Neisseria gonorrhoeae

Seq: 238 a.a.

Struc: 238 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1021/ja503093y

J Am Chem Soc 136:9938-9946 (2014)

PubMed id: 24813921

Structure of the Neisserial outer membrane protein Opa₆₀: loop flexibility essential to receptor recognition and bacterial engulfment.

D.A.Fox, P.Larsson, R.H.Lo, B.M.Kroncke, P.M.Kasson, L.Columbus.

ABSTRACT

The structure and dynamics of Opa proteins, which we report herein, are responsible for the receptor-mediated engulfment of Neisseria gonorrheae or Neisseria meningitidis by human cells and can offer deep understanding into the molecular recognition of pathogen-host receptor interactions. Such interactions are vital to understanding bacterial pathogenesis as well as the mechanism of foreign body entry to a human cell, which may provide insights for the development of targeted pharmaceutical delivery systems. The size and dynamics of the extracellular loops of Opa60 required a hybrid refinement approach wherein membrane and distance restraints were used to generate an initial NMR structural ensemble, which was then further refined using molecular dynamics in a DMPC bilayer. The resulting ensemble revealed that the extracellular loops, which bind host receptors, occupy compact conformations, interact with each other weakly, and are dynamic on the nanosecond time scale. We predict that this conformational sampling is critical for enabling diverse Opa loop sequences to engage a common set of receptors.