2B2C

Cloning, expression, characterisation and three- dimensional structure determination of the Caenorhabditis elegans spermidine synthase

Summary for 2B2C

• Entry DOI: 10.2210/pdb2b2c/pdb
• Descriptor: spermidine synthase (2 entities in total)
• Functional Keywords: beta-alpha, transferase
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 2
• Total formula weight: 70141.94

Authors

Dufe, V.T.,Luersen, K.,Eschbach, M.L.,Haider, N.,Karlberg, T.,Walter, R.D.,Al-Karadaghi, S. (deposition date: 2005-09-19, release date: 2005-11-15, Last modification date: 2024-03-13)

Primary citation

Dufe, V.T.,Luersen, K.,Eschbach, M.L.,Haider, N.,Karlberg, T.,Walter, R.D.,Al-Karadaghi, S.
Cloning, expression, characterisation and three-dimensional structure determination of Caenorhabditis elegans spermidine synthase
FEBS LETT., 579:6037-6043, 2005

PubMed Abstract: The polyamine synthesis enzyme spermidine synthase (SPDS) has been cloned from the model nematode Caenorhabditis elegans. Biochemical characterisation of the recombinantly expressed protein revealed a high degree of similarity to other eukaryotic SPDS with the exception of a low affinity towards the substrate decarboxylated S-adenosylmethionine (Km = 110 microM) and a less pronounced feedback inhibition by the second reaction product 5'-methylthioadenosine (IC50 = 430 microM). The C. elegans protein that carries a nematode-specific insertion of 27 amino acids close to its N-terminus was crystallized, leading to the first X-ray structure of a dimeric eukaryotic SPDS.

PubMed: 16226262
DOI: 10.1016/j.febslet.2005.09.050

Experimental method

X-RAY DIFFRACTION (2.5 Å)