NADP-dependent细菌酒精脱氢酶:晶体结构,cofactor-binding辅因子特异性beijerinckii梭状芽胞杆菌的抗利尿激素和Thermoanaerobacter brockii。
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Korkhin Y,卡尔布(枚)AJ,佩雷茨M,博金啊,Burstein Y, Frolow F
NADP-dependent细菌酒精脱氢酶:晶体结构,cofactor-binding辅因子特异性beijerinckii梭状芽胞杆菌的抗利尿激素和Thermoanaerobacter brockii。
J杂志。1998年5月22日,278 (5):967 - 81。
- PubMed ID
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9836873 (在PubMed]
- 文摘
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我们已经确定是nad (H)的x射线结构端依赖酒精脱氢酶Clostridiim beijerinckii (CBADH) apo和holo-enzyme形式分辨率2.15和2.05,分别holo-alcohol脱氢酶的Thermoanaerobacter brockii (TBADH)为2.5。这是第一个原核乙醇脱氢酶结构的确定以及第一NADP (H)端依赖酒精脱氢酶CBADH和TBADH 75%序列身份和三维结构非常相似。222年都是四聚体对称。单体是由两个域:cofactor-binding域和催化领域。这些由深裂的底部的一个锌原子必然催化部位。的四聚体是由两个二聚体,每个结构同源二聚体的酒精脱氢酶的脊椎动物。二聚体形成四聚体的接触表面相反interdomain间隙从而可以从四聚物的表面。四聚物包含大量的内部空腔表面与积极的潜力。分子是nad (H)绑定的interdomain裂cofactor-binding域的每个单体。 The specificity of the two bacterial alcohol dehydrogenases toward NADP(H) is determined by residues Gly198, Ser199, Arg200 and Tyr218, with the latter three making hydrogen bonds with the 2'-phosphate oxygen atoms of the cofactor. Upon NADP(H) binding to CBADH, Tyr218 undergoes a rotation of approximately 120 degrees about chi1 which facilitates stacking interactions with the adenine moiety and hydrogen bonding with one of the phosphate oxygen atoms. In apo-CBADH the catalytic zinc is tetracoordinated by side-chains of residues Cys37, His59, Asp150 and Glu60; in holo-CBADH, Glu60 is retracted from zinc in three of the four monomers whereas in holo-TBADH, Glu60 does not participate in Zn coordination. In both holo-enzymes, but not in the apo-enzyme, residues Ser39 and Ser113 are in the second coordination sphere of the catalytic zinc. The carboxyl group of Asp150 is oriented with respect to the active carbon of NADP(H) so as to form hydrogen bonds with both pro-S and pro-R hydrogen atoms.