Structure at 1.9 Å resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5

被引：45

作者：

Chen, ZW

Matsushita, K

Yamashita, T

Fujii, TA

Toyama, H

Adachi, O

Bellamy, HD

Mathews, FS ^{[1
]}

机构：

[1] Washington Univ, Sch Med, Dept Biochem & Mol Biophys, St Louis, MO 63110 USA

[2] Yamaguchi Univ, Dept Biol Chem, Yamaguchi 7538515, Japan

[3] Stanford Synchrotron Radiat Lab, Stanford, CA 94309 USA

来源：

STRUCTURE | 2002年 / 10卷 / 06期

关键词：

alcohol dehydrogenase; electron transfer; oxidation-reduction; pyrroloquinoline quinone; quinohemoprotein; x-ray crystallography;

D O I：

10.1016/S0969-2126(02)00774-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The type II quinohemoprotein alcohol dehydrogenase of Pseudomonas putida is a periplasmic enzyme that oxidizes substrate alcohols to the aldehyde and transfers electrons first to pyrroloquinoline quinone (PQQ) and then to an internal heme group. The 1.9 Angstrom resolution crystal structure reveals that the enzyme contains a large N-terminal eight-stranded beta propeller domain (similar to60 kDa) similar to methanol dehydrogenase and a small C-terminal c-type cytochrome domain (similar to10 kDa) similar to the cytochrome subunit of p-cresol methylhydoxylase. The PQQ is bound near the axis of the propeller domain about 14 Angstrom from the heme. A molecule of acetone, the product of the oxidation of isopropanol present during crystallization, appears to be bound in the active site cavity.

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页码：837 / 849

页数：13

相关论文

共 54 条

[41] Structural requirements of pyrroloquinoline quinone dependent enzymatic reactions [J].

Oubrie, A ;

Dijkstra, BW .

PROTEIN SCIENCE, 2000, 9 (07) :1265-1273

[42] PROTEIN ELECTRON-TRANSPORT - SINGLE VERSUS MULTIPLE PATHWAYS [J].

REGAN, JJ ;

RISSER, SM ;

BERATAN, DN ;

ONUCHIC, JN .

JOURNAL OF PHYSICAL CHEMISTRY, 1993, 97 (50) :13083-13088

[43] CRYSTALLIZE - A CRYSTALLOGRAPHIC SYMMETRY DISPLAY AND HANDLING SUBPACKAGE IN TOM/FRODO [J].

ROUSSEL, A ;

FONTECILLACAMPS, JC ;

CAMBILLAU, C .

JOURNAL OF MOLECULAR GRAPHICS, 1990, 8 (02) :86-&

[44] Ca2+ stabilizes the semiquinone radical of pyrroloquinoline quinone [J].

Sato, A ;

Takagi, K ;

Kano, K ;

Kato, N ;

Duine, JA ;

Ikeda, T .

BIOCHEMICAL JOURNAL, 2001, 357 :893-898

[45] Crystal structure of quinohemoprotein amine dehydrogenase from Pseudomonas putida -: Identification of a novel quinone cofactor encaged by multiple thioether cross-bridges [J].

Satoh, A ;

Kim, JK ;

Miyahara, I ;

Devreese, B ;

Vandenberghe, I ;

Hacisalihoglu, A ;

Okajima, T ;

Kuroda, S ;

Adachi, O ;

Duine, JA ;

Van Beeumen, J ;

Tanizawa, K ;

Hirotsu, K .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (04) :2830-2834

[46] EXISTENCE OF A NOVEL ENZYME, PYRROLOQUINOLINE QUINONE-DEPENDENT POLYVINYL-ALCOHOL DEHYDROGENASE, IN A BACTERIAL SYMBIONT, PSEUDOMONAS SP STRAIN VM15C [J].

SHIMAO, M ;

NINOMIYA, K ;

KUNO, O ;

KATO, N ;

SAKAZAWA, C .

APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1986, 51 (02) :268-275

[47] Thermus thermophilus cytochrome-c(552): A new highly thermostable cytochrome-c structure obtained by MAD phasing [J].

Than, ME ;

Hof, P ;

Huber, R ;

Bourenkov, GP ;

Bartunik, HD ;

Buse, G ;

Soulimane, T .

JOURNAL OF MOLECULAR BIOLOGY, 1997, 271 (04) :629-644

[48] 3 DISTINCT QUINOPROTEIN ALCOHOL DEHYDROGENASES ARE EXPRESSED WHEN PSEUDOMONAS-PUTIDA IS GROWN ON DIFFERENT ALCOHOLS [J].

TOYAMA, H ;

FUJII, A ;

MATSUSHITA, K ;

SHINAGAWA, E ;

AMEYAMA, M ;

ADACHI, O .

JOURNAL OF BACTERIOLOGY, 1995, 177 (09) :2442-2450

[49] Determination of the gene sequence and the three-dimensional structure at 2.4 angstrom resolution of methanol dehydrogenase from Methylophilus W3A1 [J].

Xia, ZX ;

Dai, WW ;

Zhang, YF ;

White, SA ;

Boyd, GD ;

Mathews, FS .

JOURNAL OF MOLECULAR BIOLOGY, 1996, 259 (03) :480-501

[50]

Yasuda M, 1996, FEMS MICROBIOL LETT, V138, P23

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