Document Detail


The crystal structure and biochemical properties of DHBPS from Streptococcus pneumoniae, a potential anti-infective target for Gram-positive bacteria.
MedLine Citation:
PMID:  23954596     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
The enzymes involved in riboflavin biosynthesis are considered to be potential anti-bacterial drug targets because these proteins are essential in bacterial pathogens but are absent in humans. 3,4-dihydroxy-2-butanone-4-phosphate synthase (DHBPS) is one of the key enzymes in the biosynthesis of riboflavin. DHBPS catalyzes the conversion of ribulose-5-phosphate (Ru5P) to 3,4-Dihydroxy-2-butanone-4-phosphate (DHBP) and formate. The purified SpDHBPS enzyme, in the presence of Mg(2+) ion, catalyzed the conversion of Ru5P to DHBP at a rate of 109nmolmin(-)(1)mg(-1) with an apparent Km value of 181μM at 37°C. Surprisingly, our experiments first revealed that DHBPS showed activity in the presence of the trivalent metal ion, Fe(3+). Furthermore, we determined the crystal structure of DHBPS from Gram-positive bacteria, Streptococcuspneumoniae, with 2.0Å resolution. The overall architecture of SpDHBPS was similar to its homologs, which comprise one β-sheet (five-stranded) and eight α-helices, adopting a three-layered α-β-α sandwich fold. Similar to the homologs, gel-filtration experiments verified that the enzyme was arranged as a dimer. Although the overall fold of DHBPS was similar, the significant structural differences between the species at the active site region may be utilized to develop antibacterial agents that are species-specific.
Authors:
Jin Li; Zhou Hua; Luo Miao; Tang Jian; Yang Wei; Zhao Shasha; Zhang Shaocheng; Guo Zhen; Zhang Hongpeng; Huang Ailong; Wang Deqiang
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-8-15
Journal Detail:
Title:  Protein expression and purification     Volume:  -     ISSN:  1096-0279     ISO Abbreviation:  Protein Expr. Purif.     Publication Date:  2013 Aug 
Date Detail:
Created Date:  2013-8-21     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9101496     Medline TA:  Protein Expr Purif     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Crown Copyright © 2013. Published by Elsevier Inc. All rights reserved.
Affiliation:
Key Laboratory of Molecular Biology on Infectious Disease, Chongqing Medical University, YiXueYuanlu-1, Chongqing 400016, People's Republic of China; Department of Laboratory Medicine, Chongqing Medical University, YiXueYuanlu-1, Chongqing 400016, People's Republic of China.
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