1x0v: Difference between revisions

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[[Image:1x0v.~~gif~~|left|200px]]

[[Image:1x0v.png|left|200px]]

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~~'''~~Crystal Structure of Homo Sapien Glycerol-3-Phosphate Dehydrogenase 1~~'''~~

===Crystal Structure of Homo Sapien Glycerol-3-Phosphate Dehydrogenase 1===

~~==Overview==~~

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~~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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_16460752}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16460752 is the PubMed ID number.

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==About this Structure==

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[[Category: Gxgxxg motif]]

[[Category: Two independent domain]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 14~~:23:34 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:58:55 2008''

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-[[Image:1x0v.gif|left|200px]]
+{{Seed}}
+[[Image:1x0v.png|left|200px]]
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 {{STRUCTURE_1x0v|  PDB=1x0v  |  SCENE=  }}
-'''Crystal Structure of Homo Sapien Glycerol-3-Phosphate Dehydrogenase 1'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16460752}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16460752 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16460752}}
 ==About this Structure==
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 [[Category: Gxgxxg motif]]
 [[Category: Two independent domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 14:23:34 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:58:55 2008''