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Purification, crystallization and preliminary crystallographic studies of plant S-adenosyl-L-homocysteine hydrolase (Lupinus luteus).
| Content Provider | Europe PMC |
|---|---|
| Author | Brzezinski, Krzysztof Bujacz, Grzegorz Jaskolski, Mariusz |
| Copyright Year | 2008 |
| Description | By degrading S-adenosyl-l-homocysteine, which is a byproduct of S-adenosyl-l-methionine-dependent methylation reactions, S-adenosyl-l-homocysteine hydrolase (SAHase) acts as a regulator of cellular methylation processes. S-Adenosyl-l-homocysteine hydrolase from the leguminose plant yellow lupin (Lupinus luteus), LlSAHase, which is composed of 485 amino acids and has a molecular weight of 55 kDa, has been cloned, expressed in Escherichia coli and purified. Crystals of LlSAHase in complex with adenosine were obtained by the hanging-drop vapour-diffusion method using 20%(w/v) PEG 4000 and 10%(v/v) 2-propanol as precipitants in 0.1 M Tris–HCl buffer pH 8.0. The crystals were tetragonal, space group P43212, with unit-cell parameters a = 122.4, c = 126.5 Å and contained two protein molecules in the asymmetric unit, corresponding to the functional dimeric form of the enzyme. Atomic resolution (1.17 Å) X-ray diffraction data have been collected using synchrotron radiation. Single crystals of recombinant S-adenosyl-l-homocysteine hydrolase from L. luteus in complex with adenosine diffract X-rays to 1.17 Å resolution at 100 K. The crystals are tetragonal, space group P43212, and contain one copy of the dimeric enzyme in the asymmetric unit. |
| Related Links | https://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC2443962&blobtype=pdf |
| Volume Number | 64 |
| PubMed Central reference number | PMC2443962 |
| Issue Number | Pt 7 |
| Issue Number | pt 7 |
| PubMed reference number | 18607106 |
| Journal | Acta Crystallogr Sect F Struct Biol Cryst Commun |
| e-ISSN | 17443091 |
| DOI | 10.1107/s1744309108017703 |
| Language | English |
| Publisher | International Union of Crystallography |
| Publisher Date | 2008-06-28 |
| Access Restriction | Open |
| Rights License | © International Union of Crystallography 2008 |
| Subject Keyword | S-adenosyl-l-homocysteine hydrolase Lupinus luteus |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry Condensed Matter Physics Genetics Biophysics Structural Biology |
