兰州大学机构库
Single-particle analysis of urea amidolyase reveals its molecular mechanism
Liu, Ying1; Yuan, Bin1; Peng, L(彭亮)1; Zhao, Jing2; Cheng, Bin1; Huang, Yuhua1; Zheng, Xinxing1; Zhou, Yuerong3; Xiang, Song2; Zhu, L(朱莉)1; Wu, Y(武一)1
2020-05
Source PublicationPROTEIN SCIENCE   Impact Factor & Quartile Of Published Year  The Latest Impact Factor & Quartile
ISSN0961-8368
EISSN1469-896X
Volume29Issue:5Pages:1242-1249
page numbers8
AbstractUrea amidolyase (UA), a bifunctional enzyme that is widely distributed in bacteria, fungi, algae, and plants, plays a pivotal role in the recycling of nitrogen in the biosphere. Its substrate urea is ultimately converted to ammonium, via successive catalysis at the C-terminal urea carboxylase (UC) domain and followed by the N-terminal allophanate hydrolyse (AH) domain. Although our previous studies have shown that Kluyveromyces lactis UA (KlUA) functions efficiently as a homodimer, the architecture of the full-length enzyme remains unresolved. Thus how the biotin carboxyl carrier protein (BCCP) domain is transferred within the UC domain remains unclear. Here we report the structures of full-length KlUA in its homodimer form in three different functional states by negatively-stained single-particle electron microscopy. We report here that the ADP-bound structure with or without urea shows two possible locations of BCCP with preferred asymmetry, and that when BCCP is attached to the carboxyl transferase domain of one monomer, it is attached to the biotin carboxylase domain in the second domain. Based on this observation, we propose a BCCP-swinging model for biotin-dependent carboxylation mechanism of this enzyme.
Keywordelectron microscopy negative staining single-particle analysis structural biology
PublisherWILEY
DOI10.1002/pro.3847
Indexed BySCIE
Language英语
Funding ProjectFundamental Research Funds for the Central Universities[lzujbky-2018-105][lzujbky-2018-it55] ; National Natural Science Foundation of China[31600593] ; Special Funding for Open and Shared Large-Scale Instruments and Equipment of Lanzhou University[LZU-GXJJ-2019C028]
WOS Research AreaBiochemistry & Molecular Biology
WOS SubjectBiochemistry & Molecular Biology
WOS IDWOS:000528725900013
PublisherWILEY
Original Document TypeArticle
PMID 32105377
Citation statistics
Document Type期刊论文
Identifierhttps://ir.lzu.edu.cn/handle/262010/368997
Collection兰州大学
生命科学学院
Corresponding AuthorZhu, Li; Wu, Yi
Affiliation
1.Lanzhou Univ, Sch Life Sci, MOE Key Lab Cell Act & Stress Adaptat, Lanzhou, Peoples R China
2.Tianjin Med Univ, Key Lab Immune Microenvironm & Dis, Minist Educ, Tianjin, Peoples R China
3.Fujian Normal Univ, Coll Marine & Biochem Engn, Fuzhou, Peoples R China
First Author AffilicationSchool of Life Sciences
Corresponding Author AffilicationSchool of Life Sciences
First Signature AffilicationSchool of Life Sciences
Recommended Citation
GB/T 7714
Liu, Ying,Yuan, Bin,Peng, Liang,et al. Single-particle analysis of urea amidolyase reveals its molecular mechanism[J]. PROTEIN SCIENCE,2020,29(5):1242-1249.
APA Liu, Ying.,Yuan, Bin.,Peng, Liang.,Zhao, Jing.,Cheng, Bin.,...&Wu, Yi.(2020).Single-particle analysis of urea amidolyase reveals its molecular mechanism.PROTEIN SCIENCE,29(5),1242-1249.
MLA Liu, Ying,et al."Single-particle analysis of urea amidolyase reveals its molecular mechanism".PROTEIN SCIENCE 29.5(2020):1242-1249.
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