title: Structural basis of CoA recognition by the Pyrococcus single-domain CoA-binding proteins.
abstract: The single-domain coenzyme A (CoA)-binding protein is conserved in bacteria, archaea, and a few eukaryal taxa. It consists of a Rossmann-fold domain, belonging to the FAD/NAD(P)-binding ;superfamily. The crystal structure of the Thermus thermophilus single-domain CoA-binding protein, TTHA1899, has been determined and it has been demonstrated, by isothermal titration calorimetry, that the protein interacts with CoA [Wada T. et al. Acta Crystallogr D Biol Crystallogr 59 (2003) 1213]. In the present study, we determined the crystal structures of an orthologous protein from the archaeon Pyrococcus horikoshii (PH1109), alone and complexed with CoA, at 1.65 A and 1.70 A resolutions, respectively, and that of P. furiosus protein (PF0725) in the CoA-bound form at 1.70 A. The CoA-bound structures are very similar to each other, revealing that the Pyrococcus proteins bind CoA in a 1:1 stoichiometry. Five loop-containing regions form the CoA-binding groove, to which the CoA molecule is docked. A comparison of the structures and the sequences of the Pyrococcus proteins with those of the T. theromphilus orthologue TTHA1899 indicated that archaeal and bacterial single-domain CoA-binding proteins share the same CoA-binding mode. Nevertheless, many of the peripheral residues involved in the hydrogen-bonding/electrostatic interactions with CoA are not strictly conserved in the family. The CoA interaction of the single-domain CoA-binding proteins is significantly different and much more extensive than that of the multi-subunit/multi-domain CoA-binding protein succinyl-CoA synthetase.
authors.affiliation: Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
authors.forename: Takuya B
authors.initials: TB
authors.lastname: Hiyama
authors.forename: Min
authors.initials: M
authors.lastname: Zhao
authors.forename: Yu
authors.initials: Y
authors.lastname: Kitago
authors.forename: Min
authors.initials: M
authors.lastname: Yao
authors.forename: Shun-Ichi
authors.initials: S
authors.lastname: Sekine
authors.forename: Takaho
authors.initials: T
authors.lastname: Terada
authors.forename: Chizu
authors.initials: C
authors.lastname: Kuroishi
authors.forename: Zhi-Jie
authors.initials: ZJ
authors.lastname: Liu
authors.forename: John P
authors.initials: JP
authors.lastname: Rose
authors.forename: Seiki
authors.initials: S
authors.lastname: Kuramitsu
authors.forename: Mikako
authors.initials: M
authors.lastname: Shirouzu
authors.forename: Nobuhisa
authors.initials: N
authors.lastname: Watanabe
authors.forename: Shigeyuki
authors.initials: S
authors.lastname: Yokoyama
authors.forename: Isao
authors.initials: I
authors.lastname: Tanaka
authors.forename: Bi-Cheng
authors.initials: BC
authors.lastname: Wang
mesh_terms: D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D003065:Coenzyme A / Q000737:chemistry / Q000378:metabolism*; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D011485:Protein Binding / Q000502:physiology; D017434:Protein Structure, Tertiary; D043902:Pyrococcus horikoshii / Q000378:metabolism*
chemical_list: D002352:Carrier Proteins; D003065:Coenzyme A