2b2c

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(New page: 200px<br /><applet load="2b2c" size="350" color="white" frame="true" align="right" spinBox="true" caption="2b2c, resolution 2.500&Aring;" /> '''Cloning, expression...)
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==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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[[Category: Spermidine synthase]]
[[Category: Spermidine synthase]]
[[Category: Al-Karadaghi, S.]]
[[Category: Al-Karadaghi, S.]]
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[[Category: Dufe, V.T.]]
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[[Category: Dufe, V T.]]
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[[Category: Eschbach, M.L.]]
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[[Category: Eschbach, M L.]]
[[Category: Haider, N.]]
[[Category: Haider, N.]]
[[Category: Karlberg, T.]]
[[Category: Karlberg, T.]]
[[Category: Luersen, K.]]
[[Category: Luersen, K.]]
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[[Category: Walter, R.D.]]
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[[Category: Walter, R D.]]
[[Category: beta-alpha]]
[[Category: beta-alpha]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:14:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:33:25 2008''

Revision as of 14:33, 21 February 2008


2b2c, resolution 2.500Å

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

Overview

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.

About this Structure

2B2C is a Single protein structure of sequence from Caenorhabditis elegans. Active as Spermidine synthase, with EC number 2.5.1.16 Full crystallographic information is available from OCA.

Reference

Cloning, expression, characterisation and three-dimensional structure determination of Caenorhabditis elegans spermidine synthase., Dufe VT, Luersen K, Eschbach ML, Haider N, Karlberg T, Walter RD, Al-Karadaghi S, FEBS Lett. 2005 Nov 7;579(27):6037-43. Epub 2005 Oct 5. PMID:16226262

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