A copper(I) protein possibly involved in the assembly of CuA center of bacterial cytochrome c oxidase

BANCI, Lucia, Ivano BERTINI, Simone CIOFI-BAFFONI, Efthalia KATSARI, Nikolaos KATSAROS, Karel KUBÍČEK and Stefano MANGANI. A copper(I) protein possibly involved in the assembly of CuA center of bacterial cytochrome c oxidase. Proceedings of the National Academy of Sciences of the USA. Washington, 2005, vol. 102, No 11, p. 3994-3999. ISSN 0027-8424.

Basic information

• Original name: A copper(I) protein possibly involved in the assembly of CuA center of bacterial cytochrome c oxidase
• Name in Czech: Cu(I) protein mající možná co do činění v uspořádávání CuA střediska bakteriální cytochrom-c oxidázy
• Authors: BANCI, Lucia (380 Italy), Ivano BERTINI (380 Italy), Simone CIOFI-BAFFONI (380 Italy), Efthalia KATSARI (300 Greece), Nikolaos KATSAROS (300 Greece), Karel KUBÍČEK (203 Czech Republic, guarantor) and Stefano MANGANI (380 Italy).
• Edition: Proceedings of the National Academy of Sciences of the USA, Washington, 2005, 0027-8424.

Other information

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: 10610 Biophysics
• Country of publisher: United States of America
• Confidentiality degree: is not subject to a state or trade secret
• WWW: URL
• Impact factor: Impact factor: 10.231
• Organization unit: Faculty of Science
• UT WoS: 000227731000021
• Keywords in English: cytochrome c oxidase assembly protein; copper protein; cupredoxin-like fold
• Tags: copper protein, cupredoxin-like fold
• Tags: International impact, Reviewed

Abstract

Sco1 and Cox17 are accessory proteins required for the correct assembly of eukaryotic cytochrome c oxidase. At variance with Sco1, Cox17 orthologs are found only in eukaryotes. We browsed bacterial genomes to search proteins functionally equivalent to Cox17, and we identified a class of proteins of unknown function displaying a conserved gene neighborhood to bacterial Sco1 genes, all sharing a potential metal binding motif H(M)X10MX21HXM. Two members of this group, DR1885 from Deinococcus radiodurans and CC3502 from Caulobacter crescentus, were expressed, and their interaction with copper was investigated. The solution structure and extended x-ray absorption fine structure data on the former protein reveal that the protein binds copper(I) through a histidine and three Mets in a cupredoxin-like fold. The surface location of the copper-binding site as well as the type of coordination are well poised for metal transfer chemistry, suggesting that DR1885 might transfer copper, taking the role of Cox17 in bacteria. On the basis of our results, a possible pathway for copper delivery to the CuA center in bacteria is proposed.

Abstract (in Czech)

Sco1 a Cox17 jsou proteiny, jež jsou potřebné pro utvoření eukaryotické cytochrom-c oxidázy. Na rozdíl od Sco1, Cox17 orthology se vyskytují jen v eukaryotech. Procházeli jsme bacteriální genom, abychom nalezli protein, jen je funkčně ekvivalentní Cox17 a identifikovali jsme skupinu proteinů neznámých funkcí se zachovaným sousedstvím ke genu bakteriálního Sco1. Všechny proteiny této skupiny mají vazebný motivH(M)X10MX21HXM. Dva proteiny z této skupiny - DR1885 z Deinococcus radiodurans a CC3502 z Caulobacter crescentus byly exprimovány a byla studována jejich interakce s měděnými ionty. NMR struktura a XAFS proteinu DR1885 ukazaly, že tento váže jedním histidinem a třemi methioniny jednomocnou měď. Umístění vazebného místa stejně jako typ koordinace naznačuje, že DR1885 může přenášet měď, tedy plnit roli Cox17 v bakterii. Na základě našich výsledků navrhujeme možný způsob přenosu mědi k CuA centru v bakterii.