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本文引用的文献

1
Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur.通过硫的反常散射直接确定的疏水蛋白胰凝乳蛋白酶原的结构。
Nature. 1981 Mar 12;290(5802):107-113. doi: 10.1038/290107a0.
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[33] AMoRe: An automated molecular replacement program package.[33] AMoRe：一个自动分子置换程序包。
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[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods.[27] 用于多同晶置换和多波长反常衍射方法的最大似然重原子参数精修
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Processing of X-ray diffraction data collected in oscillation mode.振荡模式下收集的X射线衍射数据的处理。
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Cryocooling and radiation damage in macromolecular crystallography.大分子晶体学中的低温冷却与辐射损伤
Acta Crystallogr D Biol Crystallogr. 2006 Jan;62(Pt 1):32-47. doi: 10.1107/S0907444905034207. Epub 2005 Dec 14.
6
Crystal structure and functional characterization of yeast YLR011wp, an enzyme with NAD(P)H-FMN and ferric iron reductase activities.酵母YLR011wp的晶体结构及功能特性，一种具有NAD(P)H - FMN和铁离子还原酶活性的酶
J Biol Chem. 2004 Aug 13;279(33):34890-7. doi: 10.1074/jbc.M405404200. Epub 2004 Jun 7.
7
Solving the structure of the bubble protein using the anomalous sulfur signal from single-crystal in-house Cu Kalpha diffraction data only.
Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):250-5. doi: 10.1107/S0907444903025927. Epub 2004 Jan 23.
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Structure of viscotoxin A3: disulfide location from weak SAD data.毒伞肽A3的结构：基于弱单波长反常散射数据确定二硫键位置
Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2125-32. doi: 10.1107/s0907444903018973. Epub 2003 Nov 27.
9
Studies on TPN-linked oxidations. I. Pathways of isocitrate oxidation in rat liver micochondria.全胃肠外营养相关氧化作用的研究。I. 大鼠肝脏线粒体中异柠檬酸的氧化途径。
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Phasing on anomalous signal of sulfurs: what is the limit?硫异常信号的定相：极限是什么？
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利用硫反常信号确定铜绿假单胞菌PA01中一种黄素单核苷酸还原酶的结构

Structure determination of an FMN reductase from Pseudomonas aeruginosa PA01 using sulfur anomalous signal.

作者信息

Agarwal Rakhi, Bonanno Jeffrey B, Burley Stephen K, Swaminathan Subramanyam

机构信息

Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.

出版信息

Acta Crystallogr D Biol Crystallogr. 2006 Apr;62(Pt 4):383-91. doi: 10.1107/S0907444906001600. Epub 2006 Mar 18.

DOI:10.1107/S0907444906001600
PMID:16552139
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1431508/
Abstract

The availability of high-intensity synchrotron facilities, technological advances in data-collection techniques and improved data-reduction and crystallographic software have ushered in a new era in high-throughput macromolecular crystallography. Here, the de novo automated crystal structure determination at 1.28 A resolution of an NAD(P)H-dependent FMN reductase flavoprotein from Pseudomonas aeruginosa PA01-derived protein Q9I4D4 using the anomalous signal from an unusually small number of S atoms is reported. Although this protein lacks the flavodoxin key fingerprint motif [(T/S)XTGXT], it has been confirmed to bind flavin mononucleotide and the binding site was identified via X-ray crystallography. This protein contains a novel flavin mononucleotide-binding site GSLRSGSYN, which has not been previously reported. Detailed statistics pertaining to sulfur phasing and other factors contributing to structure determination are discussed. Structural comparisons of the apoenzyme and the protein complexed with flavin mononucleotide show conformational changes on cofactor binding. NADPH-dependent activity has been confirmed with biochemical assays.

摘要

高强度同步加速器设施的出现、数据收集技术的技术进步以及改进的数据处理和晶体学软件，开创了高通量大分子晶体学的新纪元。本文报道了利用来自异常少量硫原子的反常信号，对源自铜绿假单胞菌PA01的蛋白质Q9I4D4的NAD(P)H依赖性FMN还原酶黄素蛋白进行1.28埃分辨率的从头自动晶体结构测定。尽管该蛋白质缺乏黄素氧还蛋白关键指纹基序[(T/S)XTGXT]，但已证实其能结合黄素单核苷酸，并通过X射线晶体学确定了结合位点。该蛋白质含有一个新的黄素单核苷酸结合位点GSLRSGSYN，此前尚未见报道。文中讨论了与硫原子相位及其他有助于结构测定的因素相关的详细统计数据。脱辅基酶与结合黄素单核苷酸的蛋白质复合物的结构比较显示辅因子结合时的构象变化。通过生化分析证实了NADPH依赖性活性。