3OND
Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with adenosine
Summary for 3OND
| Entry DOI | 10.2210/pdb3ond/pdb |
| Related | 1A7A 1B3R 1V8B 3CE6 3ONE 3ONF |
| Descriptor | Adenosylhomocysteinase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (6 entities in total) |
| Functional Keywords | plant protein, enzyme-substrate complex, nad cofactor, regulation of sam-dependent methylation reactions |
| Biological source | Lupinus luteus (European yellow lupin) |
| Total number of polymer chains | 2 |
| Total formula weight | 109620.41 |
| Authors | Brzezinski, K.,Jaskolski, M. (deposition date: 2010-08-28, release date: 2011-08-31, Last modification date: 2023-09-06) |
| Primary citation | Brzezinski, K.,Dauter, Z.,Jaskolski, M. High-resolution structures of complexes of plant S-adenosyl-L-homocysteine hydrolase (Lupinus luteus). Acta Crystallogr.,Sect.D, 68:218-231, 2012 Cited by PubMed Abstract: S-Adenosyl-L-homocysteine hydrolase (SAHase) catalyzes the reversible breakdown of S-adenosyl-L-homocysteine (SAH) to adenosine and homocysteine. SAH is formed in methylation reactions that utilize S-adenosyl-L-methionine (SAM) as a methyl donor. By removing the SAH byproduct, SAHase serves as a major regulator of SAM-dependent biological methylation reactions. Here, the first crystal structure of SAHase of plant origin, that from the legume yellow lupin (LlSAHase), is presented. Structures have been determined at high resolution for three complexes of the enzyme: those with a reaction byproduct/substrate (adenosine), with its nonoxidizable analog (cordycepin) and with a product of inhibitor cleavage (adenine). In all three cases the enzyme has a closed conformation. A sodium cation is found near the active site, coordinated by residues from a conserved loop that hinges domain movement upon reactant binding. An insertion segment that is present in all plant SAHases is located near a substrate-pocket access channel and participates in its formation. In contrast to mammalian and bacterial SAHases, the channel is open when adenosine or cordycepin is bound and is closed in the adenine complex. In contrast to SAHases from other organisms, which are active as tetramers, the plant enzyme functions as a homodimer in solution. PubMed: 22349223DOI: 10.1107/S0907444911055090 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.17 Å) |
Structure validation
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