期刊
STRUCTURE
卷 20, 期 7, 页码 1275-1284出版社
CELL PRESS
DOI: 10.1016/j.str.2012.04.016
关键词
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资金
- Biotechnology and Biological Sciences Research [H007288/1]
- Subsurface Biogeochemical Research program (SBR)/Office of Biological and Environmental Research (BER), U.S. Department of Energy (DOE)
- DOE by Battelle [DE-AC05-76RLO 1830]
- Royal Society Wolfson Foundation
- BBSRC [BB/H007288/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/H007288/1] Funding Source: researchfish
Members of the genus Shewanella translocate deca-or undeca-heme cytochromes to the external cell surface thus enabling respiration using extracellular minerals and polynuclear Fe(III) chelates. The high resolution structure of the first undeca-heme outer membrane cytochrome, UndA, reveals a crossed heme chain with four potential electron ingress/egress sites arranged within four domains. Sequence and structural alignment of UndA and the deca-heme MtrF reveals the extra heme of UndA is inserted between MtrF hemes 6 and 7. The remaining UndA hemes can be superposed over the heme chain of the decaheme MtrF, suggesting that a ten heme core is conserved between outer membrane cytochromes. The UndA structure has also been crystal-lographically resolved in complex with substrates, an Fe(III)-nitrilotriacetate dimer or an Fe(III)-citrate trimer. The structural resolution of these UndA-Fe(III)-chelate complexes provides a rationale for previous kinetic measurements on UndA and other outer membrane cytochromes.
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