The crystal structure of the beta-lactamase of Streptomyces albus G at 0.3 nm resolution - PubMed (original) (raw)
The crystal structure of the beta-lactamase of Streptomyces albus G at 0.3 nm resolution
O Dideberg et al. Biochem J. 1987.
Abstract
The crystal structure of the beta-lactamase of Streptomyces albus G has been solved at 0.3 nm resolution by X-ray-diffraction methods. The enzyme is a typical two-domain protein. One domain consists of five alpha-helices, and the other is five-stranded beta-sheet with alpha-helices on both sides of the sheet. The active-site serine residue (Ser-48) is within a cleft located between the two domains.
Similar articles
- Beta-lactamase of Bacillus licheniformis 749/C at 2 A resolution.
Moews PC, Knox JR, Dideberg O, Charlier P, Frère JM. Moews PC, et al. Proteins. 1990;7(2):156-71. doi: 10.1002/prot.340070205. Proteins. 1990. PMID: 2326252 - The 4.5 A resolution structure analysis of the exocellular DD-carboxypeptidase of Streptomyces albus G.
Dideberg O, Charlier P, Dupont L, Vermeire M, Frere JM, Ghuysen JM. Dideberg O, et al. FEBS Lett. 1980 Aug 11;117(1):212-4. doi: 10.1016/0014-5793(80)80947-1. FEBS Lett. 1980. PMID: 7409166 No abstract available. - Crystal structure of a protein proteinase inhibitor, SSI (Streptomyces subtilisin inhibitor), at 4 A resolution.
Satow Y, Mitsui Y, Iitaka Y. Satow Y, et al. J Biochem. 1978 Oct;84(4):897-906. doi: 10.1093/oxfordjournals.jbchem.a132202. J Biochem. 1978. PMID: 711703 - Active-site serine mutants of the Streptomyces albus G beta-lactamase.
Jacob F, Joris B, Frère JM. Jacob F, et al. Biochem J. 1991 Aug 1;277 ( Pt 3)(Pt 3):647-52. doi: 10.1042/bj2770647. Biochem J. 1991. PMID: 1908220 Free PMC article.
Cited by
- Configurational Entropy of Folded Proteins and Its Importance for Intrinsically Disordered Proteins.
Liu M, Das AK, Lincoff J, Sasmal S, Cheng SY, Vernon RM, Forman-Kay JD, Head-Gordon T. Liu M, et al. Int J Mol Sci. 2021 Mar 26;22(7):3420. doi: 10.3390/ijms22073420. Int J Mol Sci. 2021. PMID: 33810353 Free PMC article. - Machine Learning Classification Model for Functional Binding Modes of TEM-1 β-Lactamase.
Wang F, Shen L, Zhou H, Wang S, Wang X, Tao P. Wang F, et al. Front Mol Biosci. 2019 Jul 9;6:47. doi: 10.3389/fmolb.2019.00047. eCollection 2019. Front Mol Biosci. 2019. PMID: 31355207 Free PMC article. - Variations within class-A β-lactamase physiochemical properties reflect evolutionary and environmental patterns, but not antibiotic specificity.
Verma D, Jacobs DJ, Livesay DR. Verma D, et al. PLoS Comput Biol. 2013;9(7):e1003155. doi: 10.1371/journal.pcbi.1003155. Epub 2013 Jul 18. PLoS Comput Biol. 2013. PMID: 23874193 Free PMC article. - Molecular dynamics of class A β-lactamases-effects of substrate binding.
Fisette O, Gagné S, Lagüe P. Fisette O, et al. Biophys J. 2012 Oct 17;103(8):1790-801. doi: 10.1016/j.bpj.2012.09.009. Epub 2012 Oct 16. Biophys J. 2012. PMID: 23083723 Free PMC article. - Analysis of the plasticity of location of the Arg244 positive charge within the active site of the TEM-1 beta-lactamase.
Marciano DC, Brown NG, Palzkill T. Marciano DC, et al. Protein Sci. 2009 Oct;18(10):2080-9. doi: 10.1002/pro.220. Protein Sci. 2009. PMID: 19672877 Free PMC article.
References
- J Mol Biol. 1968 Apr 28;33(2):491-7 - PubMed
- J Mol Biol. 1976 Jul 15;104(4):865-75 - PubMed
- Methods Biochem Anal. 1976;23(0):249-345 - PubMed
- J Mol Biol. 1978 Apr 15;120(3):447-9 - PubMed
- Biochem J. 1981 Jan 1;193(1):75-82 - PubMed