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- SASDBV5: Cyclopentadecanone monooxygenase, NADP+, wild-type -

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Basic information

Entry
Database: SASBDB / ID: SASDBV5
SampleCyclopentadecanone monooxygenase, NADP+, wild-type
  • Cyclopentadecanone 1,2-monooxygenase (protein), Pseudomonas sp. HI-70
Function / homologyPyridine nucleotide-disulphide oxidoreductase / : / monooxygenase activity / FAD/NAD(P)-binding domain superfamily / Cyclopentadecanone 1,2-monooxygenase
Function and homology information
Biological speciesPseudomonas sp. HI-70 (bacteria)
CitationJournal: Biochim Biophys Acta / Year: 2016
Title: The role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure.
Authors: Brahm J Yachnin / Peter C K Lau / Albert M Berghuis /
Abstract: BACKGROUND: The Baeyer-Villiger monooxygenases (BMVOs) are a group of microbial enzymes that have garnered interest as industrial biocatalysts. While great strides have been made in recent years to ...BACKGROUND: The Baeyer-Villiger monooxygenases (BMVOs) are a group of microbial enzymes that have garnered interest as industrial biocatalysts. While great strides have been made in recent years to understand the mechanism of these enzymes from a structural perspective, our understanding remains incomplete. In particular, the role of a twenty residue loop (residues 487-504), which we refer to as the "Control Loop," that is observed in either an ordered or disordered state in various crystal structures remains unclear.
METHODS: Using SAXS, we have made the first observations of the Loop in solution with two BVMOs, cyclohexanone monooxygenase (CHMO) and cyclopentadecanone monooxygenase. We also made a series of ...METHODS: Using SAXS, we have made the first observations of the Loop in solution with two BVMOs, cyclohexanone monooxygenase (CHMO) and cyclopentadecanone monooxygenase. We also made a series of mutants of CHMO and analyzed them using SAXS, ITC, and an uncoupling assay.
RESULTS: These experiments show that Control Loop ordering results in an overall more compact enzyme without altering global protein foldedness. We have also demonstrated that the Loop plays a ...RESULTS: These experiments show that Control Loop ordering results in an overall more compact enzyme without altering global protein foldedness. We have also demonstrated that the Loop plays a critical and complex role on enzyme structure and catalysis. The Control Loop appears to have a direct impact on the organization of the overall structure of the protein, as well as in influencing the active site environment.
CONCLUSIONS: The data imply that the Loop can be divided into two regions, referred to as "sub-loops," that coordinate overall domain movements to changes in the active site.
GENERAL SIGNIFICANCE: A better understanding of the mechanistic role of the Control Loop may ultimately be helpful in designing mutants with altered specificity and improved catalytic efficiency.
Contact author
  • Albert Berghuis (McGill, McGill University, Montreal, Quebec, Canada)

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Structure visualization

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Models

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Sample

SampleName: Cyclopentadecanone monooxygenase, NADP+, wild-type / Specimen concentration: 2.25-9.00
BufferName: 50 mM Tris 2 mM TCEP 5 mM NADP+ / pH: 8
Entity #362Type: protein / Description: Cyclopentadecanone 1,2-monooxygenase / Formula weight: 69.13 / Num. of mol.: 1 / Source: Pseudomonas sp. HI-70 / References: UniProt: T2HVF7
Sequence: GSLEASMHMS QLIQEPAEAG VTSQKVSFDH VALREKYRQE RDKRLRQDGQ EQYLEVAVTC DEYLKDPYAD PIVRDPVVRE TDVFIIGGGF GGLLAAVRLQ QAGVSDYVMV ERAGDYGGTW YWNRYPGAQC DIESYVYMPL LEEMGYIPTE KYAFGTEILE YSRSIGRKFG ...Sequence:
GSLEASMHMS QLIQEPAEAG VTSQKVSFDH VALREKYRQE RDKRLRQDGQ EQYLEVAVTC DEYLKDPYAD PIVRDPVVRE TDVFIIGGGF GGLLAAVRLQ QAGVSDYVMV ERAGDYGGTW YWNRYPGAQC DIESYVYMPL LEEMGYIPTE KYAFGTEILE YSRSIGRKFG LYERTYFQTE VKDLSWDDEA ARWRITTDRG DKFSARFVCM STGPLQRPKL PGIPGITSFK GHSFHTSRWD YSYTGGDQTG NLEGLKDKRV AIIGTGATSI QAVPHLAAYA QELYVIQRTP ISVGFRGNKP TDPEWAKSLQ PGWQQARMDN FNAITHGMPV DVDLVQDSWT KIFGEIGVFL GSDGSRAQMV DFQLMEQIRA RVDQEVKDPA TAESLKPYYN IMCKRPGFHD SYLPSFNKPN VTLVDTQGAG VERITEKGLV VNGREYEVDC LIYATGFEYQ TKLSRRNGYE IHGRNGQPLS DKWKDGLSTL WGYHIRDFPN CFILGNGQSA VTPNFTHMLN EAGKHVAYVV KHCLDERVDV FEPTAEAEQA WVDHVMSFAG IKQQYDRECT PSYYNNEGQV NDVALTRNNF YPGGAVAFIN ILREWREKGD FAQFQQRKR

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Experimental information

BeamInstrument name: Advanced Light Source (ALS) 12.3.1 (SIBYLS)
City: Berkeley, CA / 国: USA / Type of source: X-ray synchrotron / Wavelength: 0.1 Å / Dist. spec. to detc.: 1.5 mm
DetectorName: MAR 165 CCD
Scan
Title: Cyclopentadecanone monooxygenase, NADP+, wild-type / Measurement date: Oct 2, 2012 / Cell temperature: 20 °C / Number of frames: 4 / Unit: 1/A /
MinMax
Q0.0222 0.3135
Distance distribution function P(R)
Sofotware P(R): GNOM 4.6 / Number of points: 480 /
MinMax
Q0.0222 0.3135
P(R) point1 480
R0 87
Result
D max: 8.7 / Type of curve: merged
ExperimentalStandardPorod
MW69.13 kDa72.1 kDa-
Volume--120 nm3

P(R)Guinier
Forward scattering, I01922 1937
Radius of gyration, Rg2.622 nm2.658 nm

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