| Local structure investigation of the active site of the imidazolonepropionase from Bacillus subtilis by XANES spectroscopy and ab initio calculations. | |
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MedLine Citation:
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PMID: 18296777 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Imidazolonepropionase is an important enzyme that plays a crucial role in the degradation of the histidine in mammals and bacteria. In this contribution a detailed structural investigation is presented of the imidazolonepropionase from Bacillus subtilis at the zinc site by X-ray absorption near-edge structure (XANES) spectroscopy combining experimental data with ab initio calculation in the framework of the multiple-scattering theory. The resolved local structure leads to a modification of the data set in the Protein Data Bank (PDB) (PDB code 2BB0). Actually, data suggest that the carboxyl of the Asp324 moves far away from the zinc ion at the center, while the water molecule and the nearest-neighbor histidines move towards it. This new conformation and the occurrence of a short water-to-zinc bond length support the nucleophilic attack catalytic mechanism proposed for this enzyme. |
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Authors:
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Feifei Yang; Wangsheng Chu; Meijuan Yu; Yu Wang; Sixuan Ma; Yuhui Dong; Ziyu Wu |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2008-02-19 |
Journal Detail:
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Title: Journal of synchrotron radiation Volume: 15 ISSN: 0909-0495 ISO Abbreviation: J Synchrotron Radiat Publication Date: 2008 Mar |
Date Detail:
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Created Date: 2008-02-25 Completed Date: 2008-05-19 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9888878 Medline TA: J Synchrotron Radiat Country: Denmark |
Other Details:
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Languages: eng Pagination: 129-33 Citation Subset: IM |
Affiliation:
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Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, People's Republic of China. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amidohydrolases
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chemistry* Bacillus subtilis / enzymology Bacterial Proteins / chemistry* Binding Sites Computer Simulation Crystallography, X-Ray Hydrogen Bonding Models, Molecular Protein Conformation Spectrum Analysis X-Rays Zinc / chemistry |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 7440-66-6/Zinc; EC 3.5.-/Amidohydrolases; EC 3.5.2.7/imidazolonepropionase, Bacillus subtilis |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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