3QXJ

Crystal structure of dethiobiotin synthetase (BioD) from Helicobacter pylori complexed with GTP

3QXJ の概要

• エントリーDOI: 10.2210/pdb3qxj/pdb
• 関連するPDBエントリー: 2QMO 3MLE 3QXC 3QXH 3QXS 3QXX 3QY0
• 分子名称: Dethiobiotin synthetase, GUANOSINE-5'-TRIPHOSPHATE, 1,2-ETHANEDIOL, ... (6 entities in total)
• 機能のキーワード: dtbs, dethiobiotin synthetase, adp binding, structural genomics, psi-biology, protein structure initiative, midwest center for structural genomics, mcsg, ligase
• 由来する生物種: Helicobacter pylori (Campylobacter pylori)
• 細胞内の位置: Cytoplasm (By similarity): O24872
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28316.19

構造登録者

Klimecka, M.M.,Porebski, P.J.,Chruszcz, M.,Murzyn, K.,Joachimiak, A.,Minor, W.,Midwest Center for Structural Genomics (MCSG) (登録日: 2011-03-01, 公開日: 2011-03-30, 最終更新日: 2023-09-13)

主引用文献

Porebski, P.J.,Klimecka, M.,Chruszcz, M.,Nicholls, R.A.,Murzyn, K.,Cuff, M.E.,Xu, X.,Cymborowski, M.,Murshudov, G.N.,Savchenko, A.,Edwards, A.,Minor, W.
Structural characterization of Helicobacter pylori dethiobiotin synthetase reveals differences between family members.
Febs J., 279:1093-1105, 2012

PubMed Abstract: Dethiobiotin synthetase (DTBS) is involved in the biosynthesis of biotin in bacteria, fungi, and plants. As humans lack this pathway, DTBS is a promising antimicrobial drug target. We determined structures of DTBS from Helicobacter pylori (hpDTBS) bound with cofactors and a substrate analog, and described its unique characteristics relative to other DTBS proteins. Comparison with bacterial DTBS orthologs revealed considerable structural differences in nucleotide recognition. The C-terminal region of DTBS proteins, which contains two nucleotide-recognition motifs, differs greatly among DTBS proteins from different species. The structure of hpDTBS revealed that this protein is unique and does not contain a C-terminal region containing one of the motifs. The single nucleotide-binding motif in hpDTBS is similar to its counterpart in GTPases; however, isothermal titration calorimetry binding studies showed that hpDTBS has a strong preference for ATP. The structural determinants of ATP specificity were assessed with X-ray crystallographic studies of hpDTBS·ATP and hpDTBS·GTP complexes. The unique mode of nucleotide recognition in hpDTBS makes this protein a good target for H. pylori-specific inhibitors of the biotin synthesis pathway.

PubMed: 22284390
DOI: 10.1111/j.1742-4658.2012.08506.x

実験手法

X-RAY DIFFRACTION (1.38 Å)