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Crystal structures of the PLP- and PMP-bound forms of BtrR, a dual functional aminotransferase involved in butirosin biosynthesis.

Popovic B, Tang X, Chirgadze DY, Huang F, Blundell TL, Spencer JB
Proteins 65 220-30 (2006)
Cited: 12 times
EuropePMC logo PMID: 16894611

Abstract

The aminotransferase (BtrR), which is involved in the biosynthesis of butirosin, a 2-deoxystreptamine (2-DOS)-containing aminoglycoside antibiotic produced by Bacillus circulans, catalyses the pyridoxal phosphate (PLP)-dependent transamination reaction both of 2-deoxy-scyllo-inosose to 2-deoxy-scyllo-inosamine and of amino-dideoxy-scyllo-inosose to 2-DOS. The high-resolution crystal structures of the PLP- and PMP-bound forms of BtrR aminotransferase from B. circulans were solved at resolutions of 2.1 A and 1.7 A with R(factor)/R(free) values of 17.4/20.6 and 19.9/21.9, respectively. BtrR has a fold characteristic of the aspartate aminotransferase family, and sequence and structure analysis categorises it as a member of SMAT (secondary metabolite aminotransferases) subfamily. It exists as a homodimer with two active sites per dimer. The active site of the BtrR protomer is located in a cleft between an alpha helical N-terminus, a central alphabetaalpha sandwich domain and an alphabeta C-terminal domain. The structures of the PLP- and PMP-bound enzymes are very similar; however BtrR-PMP lacks the covalent bond to Lys192. Furthermore, the two forms differ in the side-chain conformations of Trp92, Asp163, and Tyr342 that are likely to be important in substrate selectivity and substrate binding. This is the first three-dimensional structure of an enzyme from the butirosin biosynthesis gene cluster.

Articles - 2c7t mentioned but not cited (3)

  1. Structure and mutagenic conversion of E1 dehydrase: at the crossroads of dehydration, amino transfer, and epimerization. Smith P, Szu PH, Bui C, Liu HW, Tsai SC. Biochemistry 47 6329-6341 (2008)
  2. The structure of RbmB from Streptomyces ribosidificus, an aminotransferase involved in the biosynthesis of ribostamycin. Zachman-Brockmeyer TR, Thoden JB, Holden HM. Protein Sci 26 1886-1892 (2017)
  3. Purification, crystallization and preliminary X-ray analysis of NtdA, a putative pyridoxal phosphate-dependent aminotransferase from Bacillus subtilis. van Straaten KE, Langill DM, Palmer DR, Sanders DA. Acta Crystallogr Sect F Struct Biol Cryst Commun 65 426-429 (2009)


Reviews citing this publication (4)

  1. Biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics. Llewellyn NM, Spencer JB. Nat Prod Rep 23 864-874 (2006)
  2. Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology. Martins LO, Durão P, Brissos V, Lindley PF. Cell Mol Life Sci 72 911-922 (2015)
  3. Aminoglycoside Antibiotics: New Insights into the Biosynthetic Machinery of Old Drugs. Kudo F, Eguchi T. Chem Rec 16 4-18 (2016)
  4. Progress in aminocyclitol biosynthesis. Mahmud T. Curr Opin Chem Biol 13 161-170 (2009)

Articles citing this publication (5)

  1. Human wild-type alanine:glyoxylate aminotransferase and its naturally occurring G82E variant: functional properties and physiological implications. Cellini B, Bertoldi M, Montioli R, Paiardini A, Borri Voltattorni C. Biochem J 408 39-50 (2007)
  2. Heterologous production of paromamine in Streptomyces lividans TK24 using kanamycin biosynthetic genes from Streptomyces kanamyceticus ATCC12853. Nepal KK, Oh TJ, Sohng JK. Mol Cells 27 601-608 (2009)
  3. Complete reconstitution of the diverse pathways of gentamicin B biosynthesis. Ban YH, Song MC, Hwang JY, Shin HL, Kim HJ, Hong SK, Lee NJ, Park JW, Cha SS, Liu HW, Yoon YJ. Nat Chem Biol 15 295-303 (2019)
  4. Identification and diversity of putative aminoglycoside-biosynthetic aminotransferase genes from deep-sea environmental DNA. Aoki R, Nagaya A, Arakawa S, Kato C, Tamegai H. Biosci Biotechnol Biochem 72 1388-1393 (2008)
  5. Obituary: Jonathan B. Spencer (1960-2008). Leadlay P. Chem Biol 15 424-426 (2008)


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