title: Solution NMR structure, backbone dynamics, and heme-binding properties of a novel cytochrome c maturation protein CcmE from Desulfovibrio vulgaris.
abstract: Cytochrome c maturation protein E, CcmE, plays an integral role in the transfer of heme to apocytochrome c in many prokaryotes and some mitochondria. A novel subclass featuring a heme-binding cysteine has been identified in archaea and some bacteria. Here we describe the solution NMR structure, backbone dynamics, and heme binding properties of the soluble C-terminal domain of Desulfovibrio vulgaris CcmE, dvCcmE'. The structure adopts a conserved β-barrel OB fold followed by an unstructured C-terminal tail encompassing the CxxxY heme-binding motif. Heme binding analyses of wild-type and mutant dvCcmE' demonstrate the absolute requirement of residue C127 for noncovalent heme binding in vitro.
authors.affiliation: Center for Advanced Biotechnology and Medicine, Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, Piscataway, New Jersey 08854, USA. jma@cabm.rutgers.edu
authors.forename: James M
authors.initials: JM
authors.lastname: Aramini
authors.forename: Keith
authors.initials: K
authors.lastname: Hamilton
authors.forename: Paolo
authors.initials: P
authors.lastname: Rossi
authors.forename: Asli
authors.initials: A
authors.lastname: Ertekin
authors.forename: Hsiau-Wei
authors.initials: HW
authors.lastname: Lee
authors.forename: Alexander
authors.initials: A
authors.lastname: Lemak
authors.forename: Huang
authors.initials: H
authors.lastname: Wang
authors.forename: Rong
authors.initials: R
authors.lastname: Xiao
authors.forename: Thomas B
authors.initials: TB
authors.lastname: Acton
authors.forename: John K
authors.initials: JK
authors.lastname: Everett
authors.forename: Gaetano T
authors.initials: GT
authors.lastname: Montelione
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D045304:Cytochromes c / Q000378:metabolism; D016969:Desulfovibrio vulgaris / Q000737:chemistry; D006418:Heme / Q000378:metabolism*; D006420:Hemeproteins / Q000737:chemistry* / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D017434:Protein Structure, Tertiary
chemical_list: D001425:Bacterial Outer Membrane Proteins; D006420:Hemeproteins; D006418:Heme; D045304:Cytochromes c