CRYSTAL-STRUCTURES AT 2.5 ANGSTROM RESOLUTION OF SERYL-TRANSFER-RNA SYNTHETASE COMPLEXED 2 ANALOGS OF SERYL ADENYLATE
CRYSTAL-STRUCTURES AT 2.5 ANGSTROM RESOLUTION OF SERYL-TRANSFER-RNA SYNTHETASE COMPLEXED 2 ANALOGS OF SERYL ADENYLATE
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DOI：
10.1126/science.8128224
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发表时间：
1994-03-11
期刊：
影响因子：
56.9
通讯作者：
CUSACK, S
中科院分区：
文献类型：
--
作者：
BELRHALI, H;YAREMCHUK, A;CUSACK, S
在2.5埃分辨率下测定了嗜热栖热菌丝氨酰-tRNA合成酶与两种不同的丝氨酰腺苷酸类似物复合的晶体结构。第一种复合物是酶和丝氨酰-异羟肟酸-AMP（腺苷一磷酸）之间的复合物，该复合物在晶体中由三磷酸腺苷（ATP）和丝氨酸异羟肟酸酶促产生，第二种复合物是丝氨酰腺苷酸的合成类似物（5 '-O-[N-（L-丝氨酰）-氨磺酰基]腺苷），它是酶的强抑制剂。两种分子以类似的方式通过氢键相互作用的网络结合在由反平行β折叠和合成酶催化结构域的周围环形成的深亲水裂缝中。一级序列中的四个区域参与相互作用，包括2类合成酶的基序2和3区域。除了丝氨酸侧链的特异性识别之外，在所有2类合成酶中的相互作用可能是相似的。
Crystal structures of seryl-tRNA synthetase from Thermus thermophilus complexed with two different analogs of seryl adenylate have been determined at 2.5 Angstrom resolution. The first complex is between the enzyme and seryl-hydroxamate-AMP (adenosine monophosphate), produced enzymatically in the crystal from adenosine triphosphate (ATP) and serine hydroxamate, and the second is with a synthetic analog of seryl adenylate (5'-O-[N-(L-seryl)-sulfamoyl]adenosine), which is a strong inhibitor of the enzyme. Both molecules are bound in a similar fashion by a network of hydrogen bond interactions in a deep hydrophilic cleft formed by the antiparallel beta sheet and surrounding loops of the synthetase catalytic domain. Four regions in the primary sequence are involved in the interactions, including the motif 2 and 3 regions of class 2 synthetases. Apart from the specific recognition of the serine side chain, the interactions are likely to be similar in all class 2 synthetases.