嗜热栖热菌HB8肽脱甲酰基酶的结晶及初步X射线晶体学分析

Crystallization and preliminary X-ray crystallographic analysis of peptide deformylase from Thermus thermophilus HB8.

作者信息

Kamo Masayuki, Kudo Norio, Lee Woo Cheol, Motoshima Hiroyuki, Tanokura Masaru

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

Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1299-300. doi: 10.1107/S0907444904010595. Epub 2004 Jun 22.

DOI:10.1107/S0907444904010595

PMID:15213398

Abstract

Peptide deformylase (PDF) is responsible for cleaving the formyl group at the N-terminus of nascent polypeptide chains in eubacteria and is essential to bacterial cell viability. A recombinant PDF of the thermophilic bacterium Thermus thermophilus HB8 has been crystallized by the hanging-drop vapour-diffusion method using PEG 4000 as a precipitant. The crystals belonged to the tetragonal space group P4(1) or P4(3), with unit-cell parameters a = b = 62.58, c = 105.27 A, and are most likely to contain two molecules in an asymmetric unit, giving a crystal volume per protein weight (V(M)) of 2.3 A(3) Da(-1) and a solvent content of 46.7%.

摘要

肽脱甲酰基酶（PDF）负责切割真细菌中新生多肽链N端的甲酰基，对细菌细胞活力至关重要。嗜热栖热菌HB8的重组PDF已通过悬滴气相扩散法，以聚乙二醇4000作为沉淀剂进行了结晶。晶体属于四方晶系空间群P4(1)或P4(3)，晶胞参数a = b = 62.58，c = 105.27 Å，一个不对称单位中很可能包含两个分子，蛋白质重量对应的晶体体积（V(M)）为2.3 Å³ Da⁻¹，溶剂含量为46.7%。