6DLL

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

Replaces:  5TTI

Summary for 6DLL

• Entry DOI: 10.2210/pdb6dll/pdb
• Descriptor: p-hydroxybenzoate hydroxylase, FLAVIN-ADENINE DINUCLEOTIDE, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: structural genomics, center for structural genomics of infectious diseases, csgid, p-hydroxybenzoate hydroxylase, fad, oxidoreductase
• Biological source: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
• Total number of polymer chains: 4
• Total formula weight: 181940.91

Authors

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) (deposition date: 2018-06-01, release date: 2018-06-13, Last modification date: 2023-10-11)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)