Crystallographic and SAXS studies of S-adenosyl-l-homocysteine hydrolase from Bradyrhizobium elkanii

IUCrJ
Tomasz ManszewskiMariusz Jaskolski

Abstract

S-Adenosyl-l-homocysteine hydrolase (SAHase) from the symbiotic bacterium Bradyrhizobium elkanii (BeSAHase) was crystallized in four ligand complexes with (i) mixed adenosine (Ado) and cordycepin (Cord; 3'-deoxyadenosine), (ii) adenine (Ade), (iii) Ado and (iv) mixed 2'-deoxyadenosine (2'-dAdo) and Ade. The crystal structures were solved at resolutions of 1.84, 1.95, 1.95 and 1.54 Å, respectively. Only the Ade complex crystallized with a dimer in the asymmetric unit, while all of the other complexes formed a crystallographically independent tetrameric assembly. In the Ado/Cord complex, adenosine is found in three subunits while the fourth subunit has cordycepin bound in the active site. In the Ade and Ado complexes only these ligand molecules are present in the active sites. The 2'-dAdo/Ade complex has Ade bound in two subunits and 2'-dAdo bound in the other two subunits. The BeSAHase fold adopted a closed conformation in the complexes with Ado, Ade and 2'-dAdo, and a semi-open conformation when cordycepin occupied the active site. An SAHase-specific molecular gate, consisting of residues His342 and Phe343, behaves differently in the different complexes, but there is no simple correlation with the ligand type. Additional small-...Continue Reading

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Citations

Aug 18, 2017·Physiologia Plantarum·Moona RahikainenSaijaliisa Kangasjärvi
Jun 19, 2019·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Peng QinDengXue Lu
Apr 6, 2018·Frontiers in Microbiology·Lyn L KailingIoannis V Pavlidis
Aug 5, 2021·Cell Reports·Kevin B KoronowskiPaolo Sassone-Corsi

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Methods Mentioned

BETA
X-ray
size-exclusion chromatography

Software Mentioned

Coot
TLSMD
elBOW
PRIMUS
CheckMyMetal ( CMM )
Phaser
XDS
CRYSOL
BeSAHase
DAMMIN

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