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本文引用的文献

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Advances in understanding the molecular basis of plant cell wall polysaccharide recognition by carbohydrate-binding modules.理解植物细胞壁多糖识别的分子基础的研究进展。
Curr Opin Struct Biol. 2013 Oct;23(5):669-77. doi: 10.1016/j.sbi.2013.05.005. Epub 2013 Jun 13.
2
Molecular approaches for ameliorating microbial xylanases.改善微生物木聚糖酶的分子方法。
Bioresour Technol. 2012 Aug;117:360-7. doi: 10.1016/j.biortech.2012.04.034. Epub 2012 Apr 21.
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REFMAC5 for the refinement of macromolecular crystal structures.用于大分子晶体结构精修的REFMAC5
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iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM.iMOSFLM：一种用于MOSFLM衍射图像处理的新图形界面。
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Carbohydrate-binding modules promote the enzymatic deconstruction of intact plant cell walls by targeting and proximity effects.碳水化合物结合模块通过靶向和邻近效应促进完整植物细胞壁的酶促解构。
Proc Natl Acad Sci U S A. 2010 Aug 24;107(34):15293-8. doi: 10.1073/pnas.1005732107. Epub 2010 Aug 9.
6
Putting an N-terminal end to the Clostridium thermocellum xylanase Xyn10B story: crystal structure of the CBM22-1-GH10 modules complexed with xylohexaose.从 N 端终结：热纤梭菌木聚糖酶 Xyn10B 的故事——CBM22-1-GH10 模块与木六糖复合物的晶体结构。
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Phaser crystallographic software.相位结晶学软件。
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Paenibacillus barcinonensis sp. nov., a xylanase-producing bacterium isolated from a rice field in the Ebro River delta.
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Xylanases, xylanase families and extremophilic xylanases.木聚糖酶、木聚糖酶家族及嗜极木聚糖酶
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含有CBM22-1-CBM22-2串联结构的巴氏芽孢杆菌木聚糖酶10C N端结构域的结晶及初步X射线衍射分析

Crystallization and preliminary X-ray diffraction analysis of the N-terminal domain of Paenibacillus barcinonensis xylanase 10C containing the CBM22-1-CBM22-2 tandem.

作者信息

Sainz-Polo María Ángela, González Beatriz, Pastor F I Javier, Sanz-Aparicio Julia

机构信息

Department of Crystallography and Structural Biology, Institute of Physical Chemistry Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain.

Department of Microbiology, Faculty of Biology, University of Barcelona, Avenida Diagonal 643, 08028 Barcelona, Spain.

出版信息

Acta Crystallogr F Struct Biol Commun. 2015 Feb;71(Pt 2):136-40. doi: 10.1107/S2053230X14027496. Epub 2015 Jan 28.

DOI:10.1107/S2053230X14027496
PMID:25664784
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4321464/
Abstract

A construct containing the CBM22-1-CBM22-2 tandem forming the N-terminal domain of Paenibacillus barcinonensis xylanase 10C (Xyn10C) has been purified and crystallized. A xylan-binding function and an affinity for mixed β-1,3/β-1,4 glucans have previously been demonstrated for some members of the CBM22 family. The sequence of the tandem is homologous to the N-terminal domains found in several thermophilic enzymes. Crystals of this tandem were grown by the streak-seeding method after a long optimization strategy. The structure has been determined by molecular replacement to a resolution of 2.43 Å and refinement is under way. This study represents the first structure containing two contiguous CBM22 modules, which will contribute to a better understanding of the role that this multiplicity plays in fine-tuning substrate affinity.

摘要

一种包含形成巴氏芽孢杆菌木聚糖酶10C（Xyn10C）N端结构域的CBM22-1-CBM22-2串联体的构建体已被纯化并结晶。先前已证明CBM22家族的一些成员具有木聚糖结合功能以及对混合β-1,3/β-1,4葡聚糖的亲和力。该串联体的序列与几种嗜热酶中发现的N端结构域同源。经过长时间的优化策略后，通过条带接种法生长出了该串联体的晶体。该结构已通过分子置换法解析到2.43 Å的分辨率，目前正在进行精修。这项研究代表了第一个包含两个相邻CBM22模块的结构，这将有助于更好地理解这种多样性在微调底物亲和力中所起的作用。