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Article

Evidence of Fe3+ interaction with the plug domain of the outer membrane transferrin receptor protein of Neisseria gonorrhoeae: implications for Fe transport.

Metallomics : integrated biometal science - 1 Apr 2012

Banerjee Sambuddha, Siburt Claire J Parker, Mistry Shreni, Noto Jennifer M, DeArmond Patrick, Fitzgerald Michael C, Lambert Lisa A, Cornelissen Cynthia N, Crumbliss Alvin L

Abstract excerpt

Neisseria gonorrhoeae is an obligate pathogen that hijacks iron from the human iron transport protein, holo-transferrin (Fe(2)-Tf), by expressing TonB-dependent outer membrane receptor proteins, TbpA and TbpB. Homologous to other TonB-dependent outer membrane transporters, TbpA is thought to consist of a β-barrel with an N-terminal plug domain. Previous reports by our laboratories show that the sequence EIEYE in...

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PMID: 22399131
DOI: 10.1039/c2mt20037f
PMCID: PMC3391718

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Evidence of Fe3+ interaction with the plug domain of the outer membrane transferrin receptor protein of Neisseria gonorrhoeae: implications for Fe transport.PMID 22399131Read ↗

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