聚酮合酶还原酶（CPR-C1）与 NADPH 复合物的晶体结构来自近平滑假丝酵母IFO0708。

Crystal structure of conjugated polyketone reductase (CPR-C1) from Candida parapsilosis IFO 0708 complexed with NADPH.

机构信息

Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.

出版信息

Proteins. 2013 Nov;81(11):2059-63. doi: 10.1002/prot.24363. Epub 2013 Aug 23.

DOI:10.1002/prot.24363

PMID:23852710

Abstract

Conjugated polyketone reductase (CPR-C1) from Candida parapsilosis IFO 0708 is a member of the aldo-keto reductase (AKR) superfamily and reduces ketopantoyl lactone to d-pantoyl lactone in a NADPH-dependent and stereospecific manner. We determined the crystal structure of CPR-C1.NADPH complex at 2.20 Å resolution. CPR-C1 adopted a triose-phosphate isomerase (TIM) barrel fold at the core of the structure in which Thr25 and Lys26 of the GXGTX motif bind uniquely to the adenosine 2'-phosphate group of NADPH. This finding provides a novel structural basis for NADPH binding of the AKR superfamily.

摘要

来自近平滑假丝酵母IFO 0708 的结合型聚酮还原酶（CPR-C1）是醛酮还原酶（AKR）超家族的成员，以 NADPH 依赖和立体特异性的方式将酮泛酰内酯还原为 D-泛酰内酯。我们测定了 CPR-C1.NADPH 复合物在 2.20 Å 分辨率下的晶体结构。CPR-C1 在结构的核心采用了三磷酸甘油醛异构酶（TIM）桶状折叠，其中 GXGTX 基序的 Thr25 和 Lys26 独特地结合 NADPH 的腺苷 2'-磷酸基团。这一发现为 AKR 超家族 NADPH 结合提供了新的结构基础。