1j3r: Difference between revisions

Revision as of 14:27, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1j3r.png

Template:STRUCTURE 1j3r

Crystal structure of Thermococcus litoralis phosphogrucose isomerase complexed with gluconate-6-phosphateCrystal structure of Thermococcus litoralis phosphogrucose isomerase complexed with gluconate-6-phosphate

Template:ABSTRACT PUBMED 12560104

About this StructureAbout this Structure

1J3R is a Single protein structure of sequence from Thermococcus litoralis. Full crystallographic information is available from OCA.

ReferenceReference

Characterization of the cupin-type phosphoglucose isomerase from the hyperthermophilic archaeon Thermococcus litoralis., Jeong JJ, Fushinobu S, Ito S, Jeon BS, Shoun H, Wakagi T, FEBS Lett. 2003 Jan 30;535(1-3):200-4. PMID:12560104

Page seeded by OCA on Tue Jul 1 14:27:37 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1j3r.jpg|left|200px]]
+{{Seed}}
+[[Image:1j3r.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1j3r|  PDB=1j3r  |  SCENE=  }}
-'''Crystal structure of Thermococcus litoralis phosphogrucose isomerase complexed with gluconate-6-phosphate'''
+===Crystal structure of Thermococcus litoralis phosphogrucose isomerase complexed with gluconate-6-phosphate===
-==Overview==
+<!--
-The gene encoding phosphoglucose isomerase was cloned from Thermococcus litoralis, and functionally expressed in Escherichia coli. The purified enzyme, a homodimer of 21.5 kDa subunits, was biochemically characterized. The inhibition constants for four competitive inhibitors were determined. The enzyme contained 1.25 mol Fe and 0.24 mol Zn per dimer. The activity was enhanced by the addition of Fe(2+), but inhibited by Zn(2+) and EDTA. Enzymes with mutations in conserved histidine and glutamate residues in their cupin motifs contained no metals, and showed large decreases in k(cat). The circular dichroism spectra of the mutant enzymes and the wild type enzyme were essentially the same but with slight differences.
+The line below this paragraph, {{ABSTRACT_PUBMED_12560104}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12560104 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12560104}}
 ==About this Structure==
@@ Line 34: / Line 38: @@
 [[Category: Iron ion]]
 [[Category: Phosphoglucose isomerase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:46:12 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 14:27:37 2008''