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Volumn 18, Issue 13, 2008, Pages 3764-3768

2-Aminopropane-1,2,3-tricarboxylic acid: Synthesis and co-crystallization with the class A β-lactamase BS3 of Bacillus licheniformis

Author keywords

Lactamase inhibitors; 2 Aminopropane 1,2,3 tricarboxylic acid; Aminocitrate BS3 complex; Glycine bis alkylation; X ray diffraction analysis

Indexed keywords

2 AMINOPROPANE 1,2,3 TRICARBOXYLIC ACID; BETA LACTAMASE; BETA LACTAMASE INHIBITOR;

EID: 44949106232     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2008.05.045     Document Type: Article
Times cited : (12)

References (38)
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    • note
    • I versus inhibitor concentration (ratios of hydrolysis in the absence and in the presence of inhibitors) gave the inhibition constant indicated in Table 2. All experiments were performed three times.
  • 28
    • 44949107596 scopus 로고    scopus 로고
    • note
    • 3,24 Typically, monoclinic crystals were obtained using the hanging drop vapor diffusion method with drops containing 5 μL of a protein solution (at a concentration of 40 mg/mL in 50 mM NaCl, 10 mM Tris buffer, pH 7.2) and 5 μL of 10% PEG 6000 in 100 mM sodium citrate buffer (pH 3.4), equilibrated against 1 mL of the latter solution at 20 °C. The BS3-isocitrate crystals were obtained in the same conditions, by replacing the citrate buffer by a 100 mM sodium isocitrate buffer at the same pH. The BS3-aminocitrate crystals were grown in drops containing 5 μL of a protein solution (at a concentration of 38 mg/mL in 50 mM NaCl, 10 mM Tris buffer, pH 7.2), 4 μL of 8% PEG 6000 in 100 mM sodium aminocitrate buffer (pH 3.4) plus 1 μL of 0.1 M urea additive, equilibrated against 1 mL of a 20% PEG 6000 solution, at 20 °C. X-ray diffraction experiments were carried out under cryogenic conditions (100 K) after transferring the crystals into a reservoir solution supplemented with 50% glycerol. The diffraction data for the BS3-isocitrate crystal were measured at ESRF (Grenoble, France) on the FIP-BM30a beamline (λ = 1.0 Å) using a MarResearch 165 mm CCD detector. Data for the BS3-aminocitrate crystal were collected with a Rigaku RU-200 rotating anode generator operating at 40 kV and 100 mA and a MarResearch Mar345 Imaging Plate (λ = 1.5418 Å). Intensities were indexed and integrated using MOSFLM version 6.01. The scaling of the intensity data was accomplished with SCALA of the CCP4 program suite and all corresponding statistics are available as Supplementary data. The atomic coordinates are available at the Protein Data Bank under the codes 1I2S (citrate), 1W7F (isocitrate) and 3B3X (aminocitrate).
  • 32
    • 44949223761 scopus 로고    scopus 로고
    • note
    • In the class C β-lactamase CMY2 of Klebsiella pneumoniae (β-lactamase structurally close to P99 enzyme), the citrate molecule seems to make a 180° rotation in the active site, in comparison with its position in the BS3 catalytic cleft (see Supplementary data). The atomic coordinates are available at the Protein Data Bank under the code 1ZC2.
  • 37
    • 44949201838 scopus 로고    scopus 로고
    • Yamamoto, H.; Koide, S.; Takayanagi, Y. PCT Int. Appl. WO 9635662, 1996.
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    • Takahashi, M. Jpn Kokai Tokkyo Koho JP 09059162, 1997.
    • Takahashi, M. Jpn Kokai Tokkyo Koho JP 09059162, 1997.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.