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	Structural insight into the catalytic mechanism of gluconate 5-dehydrogenase from streptococcus suis: crystal structures of the substrate-free and quaternary complex enzymes
	Zhang, Qiangmin1,2; Peng, Hao1; Gao, Feng1,3; Liu, Yiwei1; Cheng, Hao1,2; Thompson, John4; Gao, George F.1,5
刊名	Protein science
	2009-02-01
卷号	18期号:2页码:294-303
关键词	Streptococcus suis serotype 2 Gluconate 5-dehydrogenase (ga5dh) Quaternary complex Sdr enzymes Catalytic mechanism
ISSN号	0961-8368
DOI	10.1002/pro.32
通讯作者	Gao, george f.(gaof@im.ac.cn)
英文摘要	Gluconate 5-dehydrogenase (ga5dh) is an nadp(h)-dependent enzyme that catalyzes a reversible oxidoreduction reaction between d-gluconate and 5-keto-d-gluconate, thereby regulating the flux of this important carbon and energy source in bacteria. despite the considerable amount of physiological and biochemical knowledge of ga5dh, there is little physical or structural information available for this enzyme. to this end, we herein report the crystal structures of ga5dh from pathogenic streptococcus suis serotype 2 in both substrate-free and liganded (nadp1/d-gluconate/metalion) quaternary complex forms at 2.0 angstrom resolution. structural analysis reveals that ga5dh adopts a protein fold similar to that found in members of the short chain dehydrogenase/reductase (sdr) family, while the enzyme itself represents a previously uncharacterized member of this family. in solution, ga5dh exists as a tetramer that comprised four identical similar to 29 kda subunits. the catalytic site of ga5dh shows considerable architectural similarity to that found in other enzymes of the sdr family, but the s. suis protein contains an additional residue (arg104) that plays an important role in the binding and orientation of substrate. the quaternary complex structure provides the first clear crystallographic evidence for the role of a catalytically important serine residue and also reveals an amino acid tetrad rsyk that differs from the syk triad found in the majority of sdr enzymes. detailed analysis of the crystal structures reveals important contributions of ca(2+) ions to active site formation and of specific residues at the c-termini of subunits to tetramer assembly. because ga5dh is a potential target for therapy, our findings provide insight not only of catalytic mechanism, but also suggest a target of structure-based drug design.
WOS关键词	LUNG CARBONYL REDUCTASE ; ESCHERICHIA-COLI ; HYDROXYSTEROID DEHYDROGENASE ; 3-DIMENSIONAL STRUCTURE ; GLUCONOBACTER-OXYDANS ; ANGSTROM RESOLUTION ; SEQUENCE-ANALYSIS ; TERNARY COMPLEX ; CRYSTALLIZATION ; MUTAGENESIS
WOS研究方向	Biochemistry & Molecular Biology
WOS类目	Biochemistry & Molecular Biology
语种	英语
出版者	JOHN WILEY & SONS INC
WOS记录号	WOS:000264941500005
内容类型	期刊论文
URI标识	http://www.corc.org.cn/handle/1471x/2399471
专题	中国科学院大学
通讯作者	Gao, George F.
作者单位	1.Chinese Acad Sci, Inst Microbiol, Beijing 100101, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China 3.China Agr Univ, Coll Life Sci, Beijing 100094, Peoples R China 4.NIDCR, Microbial Biochem & Genet Unit, Oral Infect & Immun Branch, NIH,DHHS, Bethesda, MD 20892 USA 5.Chinese Acad Sci, China Japan Joint Lab Mol Immunol & Mol Immunol, Inst Microbiol, Beijing 100101, Peoples R China
推荐引用方式 GB/T 7714	Zhang, Qiangmin,Peng, Hao,Gao, Feng,et al. Structural insight into the catalytic mechanism of gluconate 5-dehydrogenase from streptococcus suis: crystal structures of the substrate-free and quaternary complex enzymes[J]. Protein science,2009,18(2):294-303.
APA	Zhang, Qiangmin.,Peng, Hao.,Gao, Feng.,Liu, Yiwei.,Cheng, Hao.,...&Gao, George F..(2009).Structural insight into the catalytic mechanism of gluconate 5-dehydrogenase from streptococcus suis: crystal structures of the substrate-free and quaternary complex enzymes.Protein science,18(2),294-303.
MLA	Zhang, Qiangmin,et al."Structural insight into the catalytic mechanism of gluconate 5-dehydrogenase from streptococcus suis: crystal structures of the substrate-free and quaternary complex enzymes".Protein science 18.2(2009):294-303.

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