6DLL

2.2 Angstrom Resolution Crystal Structure of P-Hydroxybenzoate Hydroxylase from Pseudomonas putida in Complex with FAD.

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6DLL の概要

• エントリーDOI: 10.2210/pdb6dll/pdb
• 分子名称: p-hydroxybenzoate hydroxylase, FLAVIN-ADENINE DINUCLEOTIDE, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: structural genomics, center for structural genomics of infectious diseases, csgid, p-hydroxybenzoate hydroxylase, fad, oxidoreductase
• 由来する生物種: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 181940.91

構造登録者

Minasov, G.,Shuvalova, L.,Kiryukhina, O.,Dubrovska, I.,Grimshaw, S.,Kwon, K.,Anderson, W.F.,Satchell, K.J.F.,Joachimiak, A.,Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2018-06-01, 公開日: 2018-06-13, 最終更新日: 2023-10-11)

主引用文献

Lazar, J.T.,Shuvalova, L.,Rosas-Lemus, M.,Kiryukhina, O.,Satchell, K.J.F.,Minasov, G.
Structural comparison of p-hydroxybenzoate hydroxylase (PobA) from Pseudomonas putida with PobA from other Pseudomonas spp. and other monooxygenases.
Acta Crystallogr.,Sect.F, 75:507-514, 2019

PubMed Abstract: The crystal structure is reported of p-hydroxybenzoate hydroxylase (PobA) from Pseudomonas putida, a possible drug target to combat tetracycline resistance, in complex with flavin adenine dinucleotide (FAD). The structure was refined at 2.2 Å resolution with four polypeptide chains in the asymmetric unit. Based on the results of pairwise structure alignments, PobA from P. putida is structurally very similar to PobA from P. fluorescens and from P. aeruginosa. Key residues in the FAD-binding and substrate-binding sites of PobA are highly conserved spatially across the proteins from all three species. Additionally, the structure was compared with two enzymes from the broader class of oxygenases: 2-hydroxybiphenyl 3-monooxygenase (HbpA) from P. nitroreducens and 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO) from Mesorhizobium japonicum. Despite having only 14% similarity in their primary sequences, pairwise structure alignments of PobA from P. putida with HbpA from P. nitroreducens and MHPCO from M. japonicum revealed local similarities between these structures. Key secondary-structure elements important for catalysis, such as the βαβ fold, β-sheet wall and α12 helix, are conserved across this expanded class of oxygenases.

PubMed: 31282871
DOI: 10.1107/S2053230X19008653

実験手法

X-RAY DIFFRACTION (2.2 Å)