1wpq
From Proteopedia
(New page: 200px<br /> <applet load="1wpq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wpq, resolution 2.5Å" /> '''Ternary Complex Of G...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1wpq.gif|left|200px]]<br /> | + | [[Image:1wpq.gif|left|200px]]<br /><applet load="1wpq" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1wpq" size=" | + | |
caption="1wpq, resolution 2.5Å" /> | caption="1wpq, resolution 2.5Å" /> | ||
'''Ternary Complex Of Glycerol 3-phosphate Dehydrogenase 1 with NAD and dihydroxyactone'''<br /> | '''Ternary Complex Of Glycerol 3-phosphate Dehydrogenase 1 with NAD and dihydroxyactone'''<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== | ||
| - | 1WPQ 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, 13P and NAD as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | + | 1WPQ 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>, <scene name='pdbligand=13P:'>13P</scene> and <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1WPQ OCA]. |
==Reference== | ==Reference== | ||
| Line 26: | Line 25: | ||
[[Category: nad]] | [[Category: nad]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:46:53 2008'' |
Revision as of 13:46, 21 February 2008
|
Ternary Complex Of Glycerol 3-phosphate Dehydrogenase 1 with NAD and dihydroxyactone
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
1WPQ is a Single protein structure of sequence from Homo sapiens with , and as ligands. 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
Page seeded by OCA on Thu Feb 21 15:46:53 2008
Categories: Glycerol-3-phosphate dehydrogenase (NAD(+)) | Homo sapiens | Single protein | Han, X. | Ou, X. | Rao, Z. | 13P | NAD | SO4 | Dehydrogenase | Dihydroxyactone complex | Gpd1 | Nad
