Structures of OppA and PstS from Yersinia pestis indicate variability of interactions with transmembrane domains [0.03%]
来自耶尔森氏鼠疫菌的OppA和PstS结构表明与跨膜区城的相互作用具有多变性
Mikio Tanabe,Osman Mirza,Thomas Bertrand et al.
Mikio Tanabe et al.
Bacterial ATP-binding cassette (ABC) transport systems couple ATP hydrolysis with the uptake and efflux of a wide range of substances across bacterial membranes. These systems are comprised of transmembrane domains, nucleotide binding domai...
Neutron and X-ray structural studies of short hydrogen bonds in photoactive yellow protein (PYP) [0.03%]
光电黄色蛋白(PYP)中短氢键的中子和X射线结构研究
S Z Fisher,S Anderson,R Henning et al.
S Z Fisher et al.
Photoactive yellow protein (PYP) from Halorhodospira halophila is a soluble 14 kDa blue-light photoreceptor. It absorbs light via its para-coumaric acid chromophore (pCA), which is covalently attached to Cys69 and is believed to be involved...
Structure and activity of Yersinia pestis 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase as a novel target for the development of antiplague therapeutics [0.03%]
鼠疫耶尔森菌6-羟甲基-7,8-二氢蝶啶焦磷酸激酶的结构与活性：作为开发抗鼠疫药物的新靶点
Jaroslaw Blaszczyk,Yue Li,Scott Cherry et al.
Jaroslaw Blaszczyk et al.
6-Hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) is a key enzyme in the folate-biosynthetic pathway and is essential for microorganisms but absent from mammals. HPPK catalyzes Mg(2+)-dependent pyrophosphoryl transfer from ATP to 6...
Conformation families of protein fragments in multidimensional torsion-angle space [0.03%]
多维扭转角空间中蛋白质片段的构象族类
Frantisek Pavelcik,Pamela Pavelcikova
Frantisek Pavelcik
Protein conformation families for automatic model building were determined for dipeptidic, tripeptidic, tetrapeptidic and pentapeptidic fragments. Mapping in n-dimensional conformational space (n = 2, 4 and 6), a conformation-generator meth...
tRNASer acceptor stem: conformation and hydration of a microhelix in a crystal structure at 1.8 A resolution [0.03%]
低分辨率晶形结构中的微小发卡结构的例子：tRNASer受体茎的构象和水合状态
Charlotte Förster,Arnd B E Brauer,Svenja Brode et al.
Charlotte Förster et al.
The crystal structure of a serine-specific tRNA acceptor-stem microhelix, the binding site for the seryl-tRNA synthetase, was solved by X-ray analysis. This seven-base-pair tRNA(Ser) microhelix forms endless rows of helices in the crystal l...
Changes to crystals of Escherichia coli beta-galactosidase during room-temperature/low-temperature cycling and their relation to cryo-annealing [0.03%]
室温/低温循环过程中大肠杆菌β-半乳糖苷酶蛋白晶体的变化及其与冷冻退火的关系
Douglas H Juers,Jeffrey Lovelace,Henry D Bellamy et al.
Douglas H Juers et al.
Flash-cooling of macromolecular crystals often compromises diffraction quality by increasing the mosaicity. In some cases, cycling the crystal between low temperature (LT) and room temperature (RT) can reverse this increase in mosaicity. Pr...
Estimates of the twinning fraction for macromolecular crystals using statistical models accounting for experimental errors [0.03%]
一种统计模型估计适用于考虑实验误差的宏观分子晶体孪晶分数的方法
Vladimir Y Lunin,Natalia L Lunina,Manfred W Baumstark
Vladimir Y Lunin
An advanced statistical model is suggested that is designed to estimate the twinning fraction in merohedrally (or pseudo-merohedrally) twinned crystals. The model takes experimental errors of the measured intensities into account and is ada...
Use of a 'caged' analogue to study the traffic of choline within acetylcholinesterase by kinetic crystallography [0.03%]
利用动力学晶体学研究乙酰胆碱酯酶中的胆碱传输——以“笼型”类似物为工具
Jacques-Philippe Colletier,Antoine Royant,Alexandre Specht et al.
Jacques-Philippe Colletier et al.
Acetylcholinesterase plays a crucial role in nerve-impulse transmission at cholinergic synapses. The apparent paradox that it displays high turnover despite its active site being buried raises cogent questions as to how the traffic of subst...
Structure of the RuBisCO chaperone RbcX from Synechocystis sp. PCC6803 [0.03%]
来源于Synechocystis sp. PCC6803的RuBisCO伴侣蛋白RbcX的结构
Shiho Tanaka,Michael R Sawaya,Cheryl A Kerfeld et al.
Shiho Tanaka et al.
In some cyanobacteria, the genes for the large and small subunits of the enzyme RuBisCO are separated on the bacterial chromosome by the insertion of a gene coding for a protein designated RbcX, which acts as a chaperone for RuBisCO. A rece...