Structure and mechanism of a phage-encoded SAM lyase revises catalytic function of enzyme family.

Guo X, Söderholm A, Kanchugal P S, Isaksen GV, Warsi O, Eckhard U, Trigüis S, Gogoll A, Jerlström-Hultqvist J, Åqvist J, Andersson DI, Selmer M
Elife 10 (2021 Feb 10)
PMID: 33567250
doi: 10.7554/eLife.61818 		Submitted to SASBDB: 2020 Jun 25
Published in SASBDB:

SASDJ55 – S-adenosylmethionine (SAM) lyase Svi3-3

Phage-encoded SAM lyase Svi3-3 (including N-terminal His6-tag and Tev cleavage site) experimental SAS data
Phage-encoded SAM lyase Svi3-3 (including N-terminal His6-tag and Tev cleavage site) Kratky plot
Sample: Phage-encoded SAM lyase Svi3-3 (including N-terminal His6-tag and Tev cleavage site) trimer, 56 kDa Unknown environmental phage protein
Buffer: 25 mM Tris-HCl, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Dec 9
RgGuinier 2.5 nm
Dmax 9.3 nm
VolumePorod 85 nm3

SASDJ65 – S-adenosylmethionine (SAM) lyase Svi3-3 in presence of SAM

Phage-encoded SAM lyase Svi3-3 (including N-terminal His6-tag and Tev cleavage site) experimental SAS data
Phage-encoded SAM lyase Svi3-3 (including N-terminal His6-tag and Tev cleavage site) Kratky plot
Sample: Phage-encoded SAM lyase Svi3-3 (including N-terminal His6-tag and Tev cleavage site) trimer, 56 kDa Unknown environmental phage protein
Buffer: 25 mM Tris-HCl, 150 mM NaCl, 5 mM SAM, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Dec 9
RgGuinier 2.5 nm
Dmax 9.1 nm
VolumePorod 89 nm3