Crystal structure of the novel PaiA N-acetyltransferase from Thermoplasma acidophilum involved in the negative control of sporulation and degradative enzyme production.
Crystal structure of the novel PaiA N-acetyltransferase from Thermoplasma acidophilum involved in the negative control of sporulation and degradative enzyme production.
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DOI：
10.1002/prot.23062
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发表时间：
2011-08
影响因子：
2.9
通讯作者：
Anderson, W. F.
中科院分区：
文献类型：
--
作者：
Filippova, E. V.;Shuvalova, L.;Minasov, G.;Kiryukhina, O.;Zhang, Y.;Clancy, S.;Radhakrishnan, I.;Joachimiak, A.;Anderson, W. F.
关键词：
与GCN5相关的N-乙酰转移酶（GNAT）是所有三个生命域中分布最广泛的乙酰转移酶系统。高酸性细菌，有它是在Apo形式中与其自然的配体（乙酰辅酶A）确定的，并与反应的乘积（辅酶A）相综合起来，与序列和结构分析相结合，表明TA0374属于Sporative of Sporation和Degr的结构。乙酰辅酶A以某种方式类似于其他gna，并且能够基于结构和对接分析的精子，预计Glu53和Tyr93是识别精子的关键。规范之间的顺序乙酰转移酶。
GCN5-related N-acetyltransferases (GNATs) are the most widely distributed acetyltransferase systems among all three domains of life. GNATs appear to be involved in several key processes, including microbial antibiotic resistance, compacting eukaryotic DNA, controlling gene expression, and protein synthesis. Here, we report the crystal structure of a putative GNAT Ta0374 from Thermoplasma acidophilum, a hyperacidophilic bacterium, that has been determined in an apo-form, in complex with its natural ligand (acetyl coenzyme A), and in complex with a product of reaction (coenzyme A) obtained by cocrystallization with spermidine. Sequence and structural analysis reveals that Ta0374 belongs to a novel protein family, PaiA, involved in the negative control of sporulation and degradative enzyme production. The crystal structure of Ta0374 confirms that it binds acetyl coenzyme A in a way similar to other GNATs and is capable of acetylating spermidine. Based on structural and docking analysis, it is expected that Glu53 and Tyr93 are key residues for recognizing spermidine. Additionally, we find that the purification His-Tag in the apo-form structure of Ta0374 prevents binding of acetyl coenzyme A in the crystal, though not in solution, and affects a chain-flip rotation of “motif A” which is the most conserved sequence among canonical acetyltransferases.
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DOI：
10.1107/s0907444903018043
发表时间：
2003-11-01
期刊：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子：
--
作者：
Grosse-Kunstleve, RW;Adams, PD
通讯作者：
Adams, PD
DOI：
10.1107/s0907444904019158
发表时间：
2004-12-01
影响因子：
2.2
作者：
Emsley, P;Cowtan, K
通讯作者：
Cowtan, K
影响因子：
4.1
作者：
Chen, Y;Vujcic, S;Porter, CW
通讯作者：
Porter, CW
DOI：
10.1107/s0907444906052024
发表时间：
2007-03-01
期刊：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子：
--
作者：
Carson, Mike;Johnson, David H.;DeLucas, Lawrence J.
通讯作者：
DeLucas, Lawrence J.
DOI：
10.1107/s0907444992007698
发表时间：
1993-01-01
期刊：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子：
--
作者：
COWTAN, KD;MAIN, P
通讯作者：
MAIN, P