Knighton D R, Bell S M, Zheng J, Ten Eyck L F, Xuong N H, Taylor S S, Sowadski J M
Department of Chemistry, University of California, San Diego, La Jolla 92093-0654, USA.
Acta Crystallogr D Biol Crystallogr. 1993 May 1;49(Pt 3):357-61. doi: 10.1107/S0907444993000502.
. A mutant (Serl39Ala) of the mouse recombinant catalytic (C) subunit of cAMP-dependent protein kinase was co-crystallized with a peptide inhibitor, PKI(5-24), and MEGA-8 (octanoyl-N-methylglucamide) detergent. This structure was refined using all observed data (30 248 reflections) between 30 and 1.95 A resolution to an R factor of 0.186. R.m.s. deviations of bond lengths and bond angles are 0.013 A and 2.3 degrees, respectively. The final model has 3075 atoms (207 solvent) with a mean B factor of 31.9 A(2). The placement of invariant protein-kinase residues and most C:PKI(5-24) interactions were confirmed, but register errors affecting residues 55-64 and 309-339 were corrected during refinement by shifting the affected sequences toward the C terminus along the previously determined backbone path. New details of C:PKI(5-24) interactions and the Ser338 autophosphorylation site are described, and the acyl group binding site near the catalytic subunit NH(2) terminus is identified.
小鼠重组环磷酸腺苷依赖性蛋白激酶催化（C）亚基的一个突变体（Ser139Ala）与一种肽抑制剂PKI(5 - 24)以及MEGA - 8（辛酰 - N - 甲基葡糖酰胺）去污剂共同结晶。利用30至1.95埃分辨率之间的所有观测数据（30248个反射）对该结构进行精修，R因子为0.186。键长和键角的均方根偏差分别为0.013埃和2.3度。最终模型有3075个原子（207个溶剂分子），平均B因子为31.9埃²。确定了不变的蛋白激酶残基的位置以及大多数C:PKI(5 - 24)相互作用，但在精修过程中，通过将受影响的序列沿先前确定的主链路径向C末端移动，纠正了影响残基55 - 64和309 - 339的配准错误。描述了C:PKI(5 - 24)相互作用和Ser338自磷酸化位点的新细节，并确定了催化亚基NH₂末端附近的酰基结合位点。
