2QMO
Crystal structure of dethiobiotin synthetase (bioD) from Helicobacter pylori
Summary for 2QMO
Entry DOI | 10.2210/pdb2qmo/pdb |
Descriptor | Dethiobiotin synthetase, CHLORIDE ION (3 entities in total) |
Functional Keywords | dethiobiotin synthetase, structural genomics, psi-2, protein structure initiative, midwest center for structural genomics, mcsg, atp-binding, biotin biosynthesis, ligase, magnesium, nucleotide-binding |
Biological source | Helicobacter pylori |
Cellular location | Cytoplasm (By similarity): O24872 |
Total number of polymer chains | 1 |
Total formula weight | 24887.91 |
Authors | Chruszcz, M.,Xu, X.,Cuff, M.,Cymborowski, M.,Zheng, H.,Savchenko, A.,Edwards, A.,Joachimiak, A.,Minor, W.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2007-07-16, release date: 2007-07-31, Last modification date: 2024-10-16) |
Primary citation | 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 Cited by 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: 22284390DOI: 10.1111/j.1742-4658.2012.08506.x PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.47 Å) |
Structure validation
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