Structural mechanism governing the quaternary organization of monocot mannose-binding lectin revealed by the novel monomeric structure of an orchid lectin

doi:10.1074/jbc.M411634200

	Structural mechanism governing the quaternary organization of monocot mannose-binding lectin revealed by the novel monomeric structure of an orchid lectin
	Liu, W ; Yang, N ; Ding, JJ ; Huang, RH ; Hu, Z ; Wang, DC
刊名	JOURNAL OF BIOLOGICAL CHEMISTRY
	2005-04-15
卷号	280 期号:15 页码:14865-14876
ISSN号	0021-9258
DOI	10.1074/jbc.M411634200
通讯作者	dcwang@sun5.ibp.ac.cn
文献子类	Article
英文摘要	Two isoforms of an antifungal protein, gastrodianin, were isolated from two subspecies of the orchid Gastrodia elata, belonging to the protein superfamily of monocot mannose-specific lectins. In the context that all available structures in this superfamily are oligomers so far, the crystal structures of the orchid lectins, both at 2.0 angstrom, revealed a novel monomeric structure. It resulted from the rearrangement of the C-terminal peptide inclusive of the 12th beta-strand, which changes from the "C-terminal exchange" into a "C-terminal self-assembly" mode. Thus, the overall tertiary scaffold is stabilized with an intramolecular beta-sheet instead of the hybrid observed on subunit/subunit interface in all known homologous dimeric or tetrameric lectins. In contrast to the constrained extended conformation with a cis peptide bond between residues 98 and 99 commonly occurring in oligomers, a beta-hairpin forms from position 97 to 101 with a normal trans peptide bond at the corresponding site in gastrodianin, which determines the topology of the C-terminal peptide and thereby its unique fold pattern. Sequence and structure comparison shows that residue replacement and insertion at the position where the beta-hairpin occurs in association with cis-trans inter-conversion of the specific peptide bond (97-98) are possibly responsible for such a radical structure switch between monomers and oligomers. Moreover, this seems to be a common melody controlling the quaternary states among bulb lectins through studies on sequence alignment. The observations revealed a structural mechanism by which the quaternary organization of monocot mannose binding lectins could be governed. The mutation experiment performed on maltose-binding protein-gastrodianin fusion protein followed by a few biochemical detections provides direct evidence to support this conclusion. Potential carbohydrate recognition sites and biological implications of the orchid lectin based on its monomeric state are also discussed in this paper.
学科主题	Biochemistry & Molecular Biology
WOS关键词	SPECIES LISTERA-OVATA ; ANTIFUNGAL PROPERTIES ; GASTRODIA-ELATA ; EPIPACTIS-HELLEBORINE ; MOLECULAR REPLACEMENT ; ANGSTROM RESOLUTION ; CRYSTAL-STRUCTURE ; SNOWDROP LECTIN ; PLANT-LECTINS ; BULB LECTIN
WOS研究方向	Biochemistry & Molecular Biology
语种	英语
WOS记录号	WOS:000228236800065
公开日期	2012-07-04
内容类型	期刊论文
源URL	[http://ir.kib.ac.cn:8080/handle/151853/13467]
专题	昆明植物研究所_离退休
作者单位	1.Chinese Acad Sci, Inst Biophys, Ctr Struct & Mol Biol, Beijing 100101, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China 3.Chinese Acad Sci, Kunming Inst Bot, Kunming 650204, Peoples R China
推荐引用方式 GB/T 7714	Liu, W,Yang, N,Ding, JJ,et al. Structural mechanism governing the quaternary organization of monocot mannose-binding lectin revealed by the novel monomeric structure of an orchid lectin[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2005,280(15):14865-14876.
APA	Liu, W,Yang, N,Ding, JJ,Huang, RH,Hu, Z,&Wang, DC.(2005).Structural mechanism governing the quaternary organization of monocot mannose-binding lectin revealed by the novel monomeric structure of an orchid lectin.JOURNAL OF BIOLOGICAL CHEMISTRY,280(15),14865-14876.
MLA	Liu, W,et al."Structural mechanism governing the quaternary organization of monocot mannose-binding lectin revealed by the novel monomeric structure of an orchid lectin".JOURNAL OF BIOLOGICAL CHEMISTRY 280.15(2005):14865-14876.