2o05
From Proteopedia
(New page: 200px<br /> <applet load="2o05" size="450" color="white" frame="true" align="right" spinBox="true" caption="2o05, resolution 2.00Å" /> '''Human spermidine sy...) |
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| - | [[Image:2o05.gif|left|200px]]<br /> | + | [[Image:2o05.gif|left|200px]]<br /><applet load="2o05" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="2o05, resolution 2.00Å" /> | caption="2o05, resolution 2.00Å" /> | ||
'''Human spermidine synthase'''<br /> | '''Human spermidine synthase'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2O05 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MTA as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1ZDZ. Active as [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] Full crystallographic information is available from [http:// | + | 2O05 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MTA:'>MTA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1ZDZ. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O05 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: structural genomics consortium]] | [[Category: structural genomics consortium]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:32:00 2008'' |
Revision as of 11:32, 23 January 2008
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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 with as ligand. This structure superseeds the now removed PDB entry 1ZDZ. Active as Spermidine synthase, with EC number 2.5.1.16 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
Page seeded by OCA on Wed Jan 23 13:32:00 2008
Categories: Homo sapiens | Single protein | Spermidine synthase | Arrowsmith, C.H. | Bochkarev, A. | Edwards, A.M. | Loppnau, P. | Min, J. | Plotnikov, A.N. | SGC, Structural.Genomics.Consortium. | Sundstrom, M. | Weigelt, J. | Wu, H. | Zeng, H. | MTA | Sgc | Structural genomics | Structural genomics consortium
