1lk7
From Proteopedia
(New page: 200px<br /><applet load="1lk7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lk7, resolution 2.0Å" /> '''Structure of D-Ribose...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1lk7.jpg|left|200px]]<br /><applet load="1lk7" size=" | + | [[Image:1lk7.jpg|left|200px]]<br /><applet load="1lk7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lk7, resolution 2.0Å" /> | caption="1lk7, resolution 2.0Å" /> | ||
'''Structure of D-Ribose-5-Phosphate Isomerase from in complex with phospho-erythronic acid'''<br /> | '''Structure of D-Ribose-5-Phosphate Isomerase from in complex with phospho-erythronic acid'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A gene homologous to D-ribose-5-phosphate isomerase (EC 5.3.1.6) was found | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1LK7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with CL, NA and DER as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribose-5-phosphate_isomerase Ribose-5-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.6 5.3.1.6] Full crystallographic information is available from [http:// | + | 1LK7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=DER:'>DER</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribose-5-phosphate_isomerase Ribose-5-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.6 5.3.1.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LK7 OCA]. |
==Reference== | ==Reference== | ||
| Line 27: | Line 27: | ||
[[Category: alpha/beta structure]] | [[Category: alpha/beta structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:41 2008'' |
Revision as of 11:45, 21 February 2008
|
Structure of D-Ribose-5-Phosphate Isomerase from in complex with phospho-erythronic acid
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.
About this Structure
1LK7 is a Single protein structure of sequence from Pyrococcus horikoshii with , and as ligands. Active as Ribose-5-phosphate isomerase, with EC number 5.3.1.6 Full crystallographic information is available from OCA.
Reference
A hyperthermostable D-ribose-5-phosphate isomerase from Pyrococcus horikoshii characterization and three-dimensional structure., Ishikawa K, Matsui I, Payan F, Cambillau C, Ishida H, Kawarabayasi Y, Kikuchi H, Roussel A, Structure. 2002 Jun;10(6):877-86. PMID:12057201
Page seeded by OCA on Thu Feb 21 13:45:41 2008
