1lk5: Difference between revisions

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[[Image:1lk5.png|left|200px]]

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~~'''~~Structure of the D-Ribose-5-Phosphate Isomerase from Pyrococcus horikoshii~~'''~~

===Structure of the D-Ribose-5-Phosphate Isomerase from Pyrococcus horikoshii===

~~==Overview==~~

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~~A gene homologous~~ to ~~D-ribose-5-phosphate isomerase~~ (~~EC 5.3~~.1.~~6) was found in the genome of Pyrococcus horikoshii. D-ribose-5-phosphate isomerase (PRI~~) is ~~of particular metabolic importance since it catalyzes~~ the ~~interconversion between the ribose and ribulose forms involved in the pentose phosphate cycle and in the process of photosynthesis~~. The gene consisting of 687 bp was overexpressed in Escherichia coli, and the resulting enzyme showed activity at high temperatures with an optimum over 90 degrees C. The crystal structures of the enzyme, free and in complex with D-4-phosphoerythronic acid inhibitor, were determined. PRI is a tetramer in the crystal and in solution, and each monomer has a new fold consisting of two alpha/beta domains. The 3D structures and the characterization of different mutants indicate a direct or indirect catalytic role for the residues E107, D85, and K98.

The line below this paragraph, {{ABSTRACT_PUBMED_12057201}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12057201 is the PubMed ID number.

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==About this Structure==

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[[Category: Roussel, A.]]

[[Category: Alpha/beta structure]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ 2 23:59:53 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 21:16:52 2008''

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-[[Image:1lk5.jpg|left|200px]]
+{{Seed}}
+[[Image:1lk5.png|left|200px]]
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 {{STRUCTURE_1lk5|  PDB=1lk5  |  SCENE=  }}
-'''Structure of the D-Ribose-5-Phosphate Isomerase from Pyrococcus horikoshii'''
+===Structure of the D-Ribose-5-Phosphate Isomerase from Pyrococcus horikoshii===
-==Overview==
+<!--
-A gene homologous to D-ribose-5-phosphate isomerase (EC 5.3.1.6) was found in the genome of Pyrococcus horikoshii. D-ribose-5-phosphate isomerase (PRI) is of particular metabolic importance since it catalyzes the interconversion between the ribose and ribulose forms involved in the pentose phosphate cycle and in the process of photosynthesis. The gene consisting of 687 bp was overexpressed in Escherichia coli, and the resulting enzyme showed activity at high temperatures with an optimum over 90 degrees C. The crystal structures of the enzyme, free and in complex with D-4-phosphoerythronic acid inhibitor, were determined. PRI is a tetramer in the crystal and in solution, and each monomer has a new fold consisting of two alpha/beta domains. The 3D structures and the characterization of different mutants indicate a direct or indirect catalytic role for the residues E107, D85, and K98.
+The line below this paragraph, {{ABSTRACT_PUBMED_12057201}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12057201 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12057201}}
 ==About this Structure==
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 [[Category: Roussel, A.]]
 [[Category: Alpha/beta structure]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:59:53 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 21:16:52 2008''