2o05

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|PDB= 2o05 |SIZE=350|CAPTION= <scene name='initialview01'>2o05</scene>, resolution 2.00&Aring;
|PDB= 2o05 |SIZE=350|CAPTION= <scene name='initialview01'>2o05</scene>, resolution 2.00&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MTA:5'-DEOXY-5'-METHYLTHIOADENOSINE'>MTA</scene>
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|LIGAND= <scene name='pdbligand=MTA:5&#39;-DEOXY-5&#39;-METHYLTHIOADENOSINE'>MTA</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Spermidine_synthase Spermidine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.16 2.5.1.16]
|ACTIVITY= [http://en.wikipedia.org/wiki/Spermidine_synthase Spermidine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.16 2.5.1.16]
|GENE= SRM, SPS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= SRM, SPS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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[[Category: structural genomics consortium]]
[[Category: structural genomics consortium]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:53:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:30:06 2008''

Revision as of 13:30, 23 March 2008

Image:2o05.gif


PDB ID 2o05

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands:
Gene: SRM, SPS1 (Homo sapiens)
Activity: Spermidine synthase, with EC number 2.5.1.16
Coordinates: save as pdb, mmCIF, xml



Human spermidine synthase


Overview

Aminopropyltransferases transfer aminopropyl groups from decarboxylated S-adenosylmethionine to amine acceptors, forming polyamines. Structural and biochemical studies have been carried out with the human spermidine synthase, which is highly specific for putrescine as the amine acceptor, and the Thermotoga maritima spermidine synthase, which prefers putrescine but is more tolerant of other substrates. Comparison of the structures of the human spermidine synthase with both substrates and products with the known structure of T. maritima spermidine synthase complexed to a multisubstrate analogue inhibitor and analysis of the properties of site-directed mutants provide a general mechanistic hypothesis for the aminopropyl transfer reaction. The studies also provide a structural basis for the specificity of the spermidine synthase subclass of the aminopropyltransferase family.

About this Structure

2O05 is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1ZDZ. Full crystallographic information is available from OCA.

Reference

Structure and mechanism of spermidine synthases., Wu H, Min J, Ikeguchi Y, Zeng H, Dong A, Loppnau P, Pegg AE, Plotnikov AN, Biochemistry. 2007 Jul 17;46(28):8331-9. Epub 2007 Jun 22. PMID:17585781

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