1ky8
From Proteopedia
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'''Crystal Structure of the Non-phosphorylating glyceraldehyde-3-phosphate Dehydrogenase''' | '''Crystal Structure of the Non-phosphorylating glyceraldehyde-3-phosphate Dehydrogenase''' | ||
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==Reference== | ==Reference== | ||
The crystal structure of the allosteric non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeum Thermoproteus tenax., Pohl E, Brunner N, Wilmanns M, Hensel R, J Biol Chem. 2002 May 31;277(22):19938-45. Epub 2002 Feb 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11842090 11842090] | The crystal structure of the allosteric non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeum Thermoproteus tenax., Pohl E, Brunner N, Wilmanns M, Hensel R, J Biol Chem. 2002 May 31;277(22):19938-45. Epub 2002 Feb 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11842090 11842090] | ||
| - | [[Category: Glyceraldehyde-3-phosphate dehydrogenase (NADP(+))]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermoproteus tenax]] | [[Category: Thermoproteus tenax]] | ||
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[[Category: Pohl, E.]] | [[Category: Pohl, E.]] | ||
[[Category: Wilmanns, M.]] | [[Category: Wilmanns, M.]] | ||
| - | [[Category: | + | [[Category: Aldh]] |
| - | [[Category: | + | [[Category: Gapn]] |
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Revision as of 20:19, 2 May 2008
Crystal Structure of the Non-phosphorylating glyceraldehyde-3-phosphate Dehydrogenase
Overview
The NAD(+)-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) from the hyperthermophilic archaeum Thermoproteus tenax represents an archaeal member of the diverse superfamily of aldehyde dehydrogenases (ALDHs). GAPN catalyzes the irreversible oxidation of d-glyceraldehyde 3-phosphate to 3-phosphoglycerate. In this study, we present the crystal structure of GAPN in complex with its natural inhibitor NADP(+) determined by multiple anomalous diffraction methods. The structure was refined to a resolution of 2.4 A with an R-factor of 0.21. The overall fold of GAPN is similar to the structures of ALDHs described previously, consisting of three domains: a nucleotide-binding domain, a catalytic domain, and an oligomerization domain. Local differences in the active site are responsible for substrate specificity. The inhibitor NADP(+) binds at an equivalent site to the cosubstrate-binding site of other ALDHs and blocks the enzyme in its inactive state, possibly preventing the transition to the active conformation. Structural comparison between GAPN from the hyperthermophilic T. tenax and homologs of mesophilic organisms establishes several characteristics of thermostabilization. These include protection against heat-induced covalent modifications by reducing and stabilizing labile residues, a decrease in number and volume of empty cavities, an increase in beta-strand content, and a strengthening of subunit contacts by ionic and hydrophobic interactions.
About this Structure
1KY8 is a Single protein structure of sequence from Thermoproteus tenax. Full crystallographic information is available from OCA.
Reference
The crystal structure of the allosteric non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeum Thermoproteus tenax., Pohl E, Brunner N, Wilmanns M, Hensel R, J Biol Chem. 2002 May 31;277(22):19938-45. Epub 2002 Feb 12. PMID:11842090 Page seeded by OCA on Fri May 2 23:19:13 2008
Categories: Single protein | Thermoproteus tenax | Brunner, N. | Hensel, R. | Pohl, E. | Wilmanns, M. | Aldh | Gapn
