2C7T

CRYSTAL STRUCTURE OF THE PLP-BOUND FORM OF BTRR, A DUAL FUNCTIONAL AMINOTRANSFERASE INVOLVED IN BUTIROSIN BIOSYNTHESIS.

2C7T の概要

• エントリーDOI: 10.2210/pdb2c7t/pdb
• 関連するPDBエントリー: 2C81
• 分子名称: GLUTAMINE-2-DEOXY-SCYLLO-INOSOSE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: aminotransferase, smat, butirosin, aminoglycoside antibiotics, transferase
• 由来する生物種: BACILLUS CIRCULANS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47428.79

構造登録者

Popovic, B.,Tang, X.,Chirgadze, D.Y.,Huang, F.,Blundell, T.L.,Spencer, J.B. (登録日: 2005-11-29, 公開日: 2006-08-16, 最終更新日: 2023-12-13)

主引用文献

Popovic, B.,Tang, X.,Chirgadze, D.Y.,Huang, F.,Blundell, T.L.,Spencer, J.B.
Crystal structures of the PLP- and PMP-bound forms of BtrR, a dual functional aminotransferase involved in butirosin biosynthesis.
Proteins, 65:220-230, 2006

PubMed 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.

PubMed: 16894611
DOI: 10.1002/prot.21076

実験手法

X-RAY DIFFRACTION (2.1 Å)