Literature DB >> 19255492

Purification, crystallization and preliminary crystallographic analysis of Est-Y29: a novel oligomeric beta-lactamase.

Seungbum Kim1, Sangbum Joo, Sangyoung Yoon, Sungsoo Kim, Jongkook Moon, Yeonwoo Ryu, Kyeong Kyu Kim, T Doohun Kim.   

Abstract

beta-Lactam antibiotics such as penicillins and cephalosporins have a four-atom ring as a common element in their structure. The beta-lactamases, which catalyze the inactivation of these antibiotics, are of great interest because of their high incidence in pathogenic bacteria. A novel oligomeric class C beta-lactamase (Est-Y29) from a metagenomic library was expressed, purified and crystallized. The recombinant protein was expressed in Escherichia coli with an N-terminal 6xHis tag and purified to homogeneity. EstY-29 was crystallized and X-ray intensity data were collected to 1.49 A resolution using synchrotron radiation.

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Year:  2009        PMID: 19255492      PMCID: PMC2650449          DOI: 10.1107/S1744309109005442

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  13 in total

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5.  EstB from Burkholderia gladioli: a novel esterase with a beta-lactamase fold reveals steric factors to discriminate between esterolytic and beta-lactam cleaving activity.

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6.  Solvent content of protein crystals.

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Review 10.  The current state of multidrug-resistant gram-negative bacilli in North America.

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  1 in total

1.  Molecular Characterization of a Novel Family VIII Esterase with β-Lactamase Activity (PsEstA) from Paenibacillus sp.

Authors:  Sena Kwon; Wanki Yoo; Young-Ok Kim; Kyeong Kyu Kim; T Doohun Kim
Journal:  Biomolecules       Date:  2019-11-26
  1 in total

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