1KBW

CRYSTAL STRUCTURE OF THE SOLUBLE DOMAIN OF ANIA FROM NEISSERIA GONORRHOEAE

Summary for 1KBW

• Entry DOI: 10.2210/pdb1kbw/pdb
• Related: 1KBV
• Descriptor: Major outer membrane protein PAN 1, COPPER (II) ION (3 entities in total)
• Functional Keywords: ania, oxidoreductase
• Biological source: Neisseria gonorrhoeae
• Cellular location: Cell outer membrane; Lipid-anchor (Probable): Q02219
• Total number of polymer chains: 6
• Total formula weight: 212039.03

Authors

Boulanger, M.J.,Murphy, M.E.P. (deposition date: 2001-11-06, release date: 2001-12-05, Last modification date: 2024-05-22)

Primary citation

Boulanger, M.J.,Murphy, M.E.
Crystal structure of the soluble domain of the major anaerobically induced outer membrane protein (AniA) from pathogenic Neisseria: a new class of copper-containing nitrite reductases.
J.Mol.Biol., 315:1111-1127, 2002

PubMed Abstract: The major anaerobically induced outer membrane protein (AniA) from pathogenic Neisseria gonorrhoeae is essential for cell growth under oxygen limiting conditions in the presence of nitrite and is protective against killing by human sera. A phylogenic analysis indicates that AniA is a member of a new class of copper-containing nitrite reductases. Expression of the soluble domain of AniA yields a protein capable of reducing nitrite with specific activity of 160 units/mg, approximately 50 % of that measured for the nitrite reductase from the strong soil denitrifier Alcaligenes faecalis S-6. The crystal structure of the soluble domain of AniA was solved by molecular replacement and sixfold averaging to a resolution of 2.4 A. The nitrite soaked AniA crystal structure refined to 1.95 A reveals a bidentate mode of substrate binding to the type II copper. Despite low sequence identity (approximately 30 %), the core cupredoxin fold of AniA is similar to that found in copper-containing nitrite reductases from soil bacteria. The main structural differences are localized to two attenuated surface loops that map to deletions in the sequence alignment. In soil nitrite reductases, one of these surface loops is positioned near the type I copper site and contributes residues to the docking surface for proteaceous electron donors. In AniA, the attenuation of this loop results in a restructured hydrophobic binding surface that may be required to interact with a lipid anchored azurin. The second attenuated loop is positioned on the opposite side of AniA and may facilitate a more intimate interaction with the lipid membrane. A unique combination of structural effectors surrounding the type I copper site of sAnia contribute to a unusual visible absorption spectra with components observed previously in either green or blue type I copper sites.

PubMed: 11827480
DOI: 10.1006/jmbi.2001.5251

Experimental method

X-RAY DIFFRACTION (2.4 Å)