Crystallographic Analysis of NMN Adenylytransferases
NMN 腺苷酸转移酶的晶体学分析
基本信息
- 批准号:6752498
- 负责人:
- 金额:$ 19.5万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:2002
- 资助国家:美国
- 起止时间:2002-06-15 至 2006-05-31
- 项目状态:已结题
- 来源:
- 关键词:DNA binding proteinEscherichia coliHaemophilus influenzaeSalmonella typhimuriumX ray crystallographyadenosine triphosphatebacterial proteinscrystallizationdinucleotideenzyme mechanismenzyme substrate complexgene expressionnicotinamidenicotinamide adenine dinucleotidenicotinamide ribotidenucleotidyltransferaseoligonucleotidespolymerase chain reactionprotein purificationprotein structure functionsite directed mutagenesis
项目摘要
DESCRIPTION: (provided by applicant) Nicotinamide mononucleotide
adenylyltransferase (NMNAT) is an indispensable enzyme in the biosynthesis and
salvage of NAD and NADP in all living organisms. In prokaryotes, it is
absolutely required for cell survival, thus representing an attractive target
for designing new broad-spectrum anti-infectious pharmaceutics. There is also
considerable medical interest in human NMNAT because it catalyzes the key step
in the metabolic conversion of the antitumor drug tiazofurin to its active
form, tiazofurin adenine dinucleotide (TAD). Because of the vital roles of NAD
in the cell, adequate levels of NAD must be maintained. In bacteria, a single
protein NadR performs multiple functions in response to the cellular NAD and
ATP levels. These include a transcriptional repressor, a NMN
adenlyltransferase, and a nicotinamide ribose kinase. NadR regulates the
expression of the genes involved in both de novo biosynthesis and savage of
NAD. It also controls the uptake of NMN and its subsequent adenylation.
Structural information of NMNAT and NadR, along with their complexes with
substrates will be essential for understanding the catalysis, substrate
recognition, inhibition, as well as regulation of these important enzymes. We
have solved the crystal structure of the first bacterial NMNAT in its ligand
free form and have obtained well diffracting human NMNAT crystals. Comparison
of the bacterial and human enzyme structures will help to design specific
bacterial inhibitors with high selectivity. Additionally, we have expressed and
purified NadR proteins from S. typhimurium and H. influenzae, and the
crystallization trials are in progress. Elucidating the structures of NadR in
its various ligand-bound forms and its complex with DNA will reveal how its
conformation and function are modulated by both NAD and ATP.
说明:(由申请人提供)烟酰胺单核苷酸
项目成果
期刊论文数量(0)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
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Crystallographic Analysis of NMN Adenylytransferases
NMN 腺苷酸转移酶的晶体学分析
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6898744 - 财政年份:2002
- 资助金额:
$ 19.5万 - 项目类别:
Crystallographic Analysis of NMN Adenylytransferases
NMN 腺苷酸转移酶的晶体学分析
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6622942 - 财政年份:2002
- 资助金额:
$ 19.5万 - 项目类别:
Crystallographic Analysis of NMN Adenylytransferases
NMN 腺苷酸转移酶的晶体学分析
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$ 19.5万 - 项目类别:
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