1x0v
From Proteopedia
(New page: 200px<br /> <applet load="1x0v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x0v, resolution 2.3Å" /> '''Crystal Structure of...) |
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caption="1x0v, resolution 2.3Å" /> | caption="1x0v, resolution 2.3Å" /> | ||
'''Crystal Structure of Homo Sapien Glycerol-3-Phosphate Dehydrogenase 1'''<br /> | '''Crystal Structure of Homo Sapien Glycerol-3-Phosphate Dehydrogenase 1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Homo sapiens L-alpha-glycerol-3-phosphate dehydrogenase 1 (GPD1) catalyzes | + | Homo sapiens L-alpha-glycerol-3-phosphate dehydrogenase 1 (GPD1) catalyzes the reversible biological conversion of dihydroxyacetone (DHAP) to glycerol-3-phosphate. The GPD1 protein was expressed in Escherichia coli, and purified as a fusion protein with glutathione S-transferase. Here we report the apoenzyme structure of GPD1 determined by multiwavelength anomalous diffraction phasing, and other complex structures with small molecules (NAD+ and DHAP) by the molecular replacement method. This enzyme structure is organized into two distinct domains, the N-terminal eight-stranded beta-sheet sandwich domain and the C-terminal helical substrate-binding domain. An electrophilic catalytic mechanism by the epsilon-NH3+ group of Lys204 is proposed on the basis of the structural analyses. In addition, the inhibitory effects of zinc and sulfate on GPDHs are assayed and discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1X0V 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 SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glycerol-3-phosphate_dehydrogenase_(NAD(+)) Glycerol-3-phosphate dehydrogenase (NAD(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.8 1.1.1.8] Full crystallographic information is available from [http:// | + | 1X0V 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glycerol-3-phosphate_dehydrogenase_(NAD(+)) Glycerol-3-phosphate dehydrogenase (NAD(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.8 1.1.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X0V OCA]. |
==Reference== | ==Reference== | ||
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[[Category: two independent domains]] | [[Category: two independent domains]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:49:58 2008'' |
Revision as of 13:49, 21 February 2008
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Crystal Structure of Homo Sapien Glycerol-3-Phosphate Dehydrogenase 1
Overview
Homo sapiens L-alpha-glycerol-3-phosphate dehydrogenase 1 (GPD1) catalyzes the reversible biological conversion of dihydroxyacetone (DHAP) to glycerol-3-phosphate. The GPD1 protein was expressed in Escherichia coli, and purified as a fusion protein with glutathione S-transferase. Here we report the apoenzyme structure of GPD1 determined by multiwavelength anomalous diffraction phasing, and other complex structures with small molecules (NAD+ and DHAP) by the molecular replacement method. This enzyme structure is organized into two distinct domains, the N-terminal eight-stranded beta-sheet sandwich domain and the C-terminal helical substrate-binding domain. An electrophilic catalytic mechanism by the epsilon-NH3+ group of Lys204 is proposed on the basis of the structural analyses. In addition, the inhibitory effects of zinc and sulfate on GPDHs are assayed and discussed.
About this Structure
1X0V is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Glycerol-3-phosphate dehydrogenase (NAD(+)), with EC number 1.1.1.8 Full crystallographic information is available from OCA.
Reference
Crystal structures of human glycerol 3-phosphate dehydrogenase 1 (GPD1)., Ou X, Ji C, Han X, Zhao X, Li X, Mao Y, Wong LL, Bartlam M, Rao Z, J Mol Biol. 2006 Mar 31;357(3):858-69. Epub 2006 Jan 18. PMID:16460752
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