title: Structure of formaldehyde dehydrogenase from Pseudomonas aeruginosa: the binary complex with the cofactor NAD+.
abstract: Formaldehyde dehydrogenase (FDH) is a member of the zinc-containing medium-chain alcohol dehydrogenase family which oxidizes toxic formaldehyde to formate using NAD(+) as an electron carrier. Three-dimensional structures have been reported for FDHs from several different species. Most FDHs are dependent on glutathione for catalysis, but the enzyme from Pseudomonas putida is an exception. In this structural communication, the recombinant production, crystallization and X-ray structure determination at 2.7 Å resolution of FDH from P. aeruginosa are described. Both the tetrameric assembly and the NAD(+)-binding mode of P. aeruginosa FDH are similar to those of P. putida FDH, which is in good agreement with the high sequence identity (87.97%) between these two proteins. Preliminary enzymatic kinetics studies of P. aeruginosa FDH also revealed a conserved glutathione-independent `ping-pong' mechanism of formaldehyde oxidization.
authors.affiliation: R&D Department, Novoprotein Scientific Inc. (Shanghai), R202, Building 2, 720 Cailun Road, Shanghai 201203, People's Republic of China.
authors.forename: Yuanping
authors.initials: Y
authors.lastname: Liao
authors.forename: Shuai
authors.initials: S
authors.lastname: Chen
authors.forename: Dingli
authors.initials: D
authors.lastname: Wang
authors.forename: Wangluo
authors.initials: W
authors.lastname: Zhang
authors.forename: Shuang
authors.initials: S
authors.lastname: Wang
authors.forename: Jianfeng
authors.initials: J
authors.lastname: Ding
authors.forename: Yingming
authors.initials: Y
authors.lastname: Wang
authors.forename: Lijun
authors.initials: L
authors.lastname: Cai
authors.forename: Xiaoyuan
authors.initials: X
authors.lastname: Ran
authors.forename: Xinquan
authors.initials: X
authors.lastname: Wang
authors.forename: Huaxing
authors.initials: H
authors.lastname: Zhu
mesh_terms: D000445:Aldehyde Oxidoreductases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D020134:Catalytic Domain; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D005557:Formaldehyde / Q000737:chemistry* / Q000378:metabolism; D007700:Kinetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009243:NAD / Q000737:chemistry* / Q000378:metabolism; D010084:Oxidation-Reduction; D011485:Protein Binding; D055503:Protein Multimerization; D011550:Pseudomonas aeruginosa / Q000737:chemistry* / Q000201:enzymology / Q000235:genetics; D016958:Pseudomonas putida / Q000737:chemistry / Q000201:enzymology / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D040681:Structural Homology, Protein
chemical_list: D001426:Bacterial Proteins; D011994:Recombinant Proteins; D009243:NAD; D005557:Formaldehyde; D000445:Aldehyde Oxidoreductases; C087006:formaldehyde dehydrogenase, glutathione-independent
keywords: NAD+; Pseudomonas aeruginosa; formaldehyde dehydrogenase