Park Jimin, Kim Hyojin, Kim Suwon, Lee Daeun, Kim Mi-Sun, Shin Dong Hae
College of Pharmacy, Ewha W. University, Seoul, Republic of Korea.
Proteins. 2018 Jan;86(1):124-131. doi: 10.1002/prot.25398. Epub 2017 Oct 31.
The crystal structure of HldC from B. pseudomallei (BpHldC), the fourth enzyme of the heptose biosynthesis pathway, has been determined. BpHldC converts ATP and d-glycero-β-d-manno-heptose-1-phosphate into ADP-d-glycero-β-d-manno-heptose and pyrophosphate. The crystal structure of BpHldC belongs to the nucleotidyltransferase α/β phosphodiesterase superfamily sharing a common Rossmann-like α/β fold with a conserved T/HXGH sequence motif. The invariant catalytic key residues of BpHldC indicate that the core catalytic mechanism of BpHldC may be similar to that of other closest homologues. Intriguingly, a reorientation of the C-terminal helix seems to guide open and close states of the active site for the catalytic reaction.
已确定来自类鼻疽杆菌（BpHldC）的庚糖生物合成途径的第四种酶HldC的晶体结构。BpHldC将ATP和d-甘油-β-d-甘露庚糖-1-磷酸转化为ADP-d-甘油-β-d-甘露庚糖和焦磷酸。BpHldC的晶体结构属于核苷酸转移酶α/β磷酸二酯酶超家族，与保守的T/HXGH序列基序共享常见的类Rossmann α/β折叠。BpHldC不变的催化关键残基表明，BpHldC的核心催化机制可能与其他最接近的同源物相似。有趣的是，C端螺旋的重新定向似乎指导了催化反应活性位点的打开和关闭状态。
