This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1x82

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1x82.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1x82.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1x82| PDB=1x82 | SCENE= }}
{{STRUCTURE_1x82| PDB=1x82 | SCENE= }}
-
'''CRYSTAL STRUCTURE OF PHOSPHOGLUCOSE ISOMERASE FROM PYROCOCCUS FURIOSUS WITH BOUND 5-phospho-D-arabinonate'''
+
===CRYSTAL STRUCTURE OF PHOSPHOGLUCOSE ISOMERASE FROM PYROCOCCUS FURIOSUS WITH BOUND 5-phospho-D-arabinonate===
-
==Overview==
+
<!--
-
Pyrococcus furiosus phosphoglucose isomerase (PfPGI) is a metal-containing enzyme that catalyses the interconversion of glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P). The recent structure of PfPGI has confirmed the hypothesis that the enzyme belongs to the cupin superfamily and identified the position of the active site. This fold is distinct from the alphabetaalpha sandwich fold commonly seen in phosphoglucose isomerases (PGIs) that are found in bacteria, eukaryotes and some archaea. Whilst the mechanism of the latter family is thought to proceed through a cis-enediol intermediate, analysis of the structure of PfPGI in the presence of inhibitors has led to the suggestion that the mechanism of this enzyme involves the metal-dependent direct transfer of a hydride between C1 and C2 atoms of the substrate. To gain further insight in the reaction mechanism of PfPGI, the structures of the free enzyme and the complexes with the inhibitor, 5-phospho-d-arabinonate (5PAA) in the presence and absence of metal have been determined. Comparison of these structures with those of equivalent complexes of the eukaryotic PGIs reveals similarities at the active site in the disposition of possible catalytic residues. These include the presence of a glutamic acid residue, Glu97 in PfPGI, which occupies the same position relative to the inhibitor as that of the glutamate that is thought to function as the catalytic base in the eukaryal-type PGIs. These similarities suggest that aspects of the catalytic mechanisms of these two structurally unrelated PGIs may be similar and based on an enediol intermediate.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15465052}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15465052 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15465052}}
==About this Structure==
==About this Structure==
Line 41: Line 45:
[[Category: Phosphoglucose isomerase]]
[[Category: Phosphoglucose isomerase]]
[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:41:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:16:57 2008''

Revision as of 06:17, 28 July 2008

Image:1x82.png

Template:STRUCTURE 1x82

CRYSTAL STRUCTURE OF PHOSPHOGLUCOSE ISOMERASE FROM PYROCOCCUS FURIOSUS WITH BOUND 5-phospho-D-arabinonate

Template:ABSTRACT PUBMED 15465052

About this Structure

1X82 is a Single protein structure of sequence from Pyrococcus furiosus. This structure supersedes the now removed PDB entry 1plz. Full crystallographic information is available from OCA.

Reference

The structures of inhibitor complexes of Pyrococcus furiosus phosphoglucose isomerase provide insights into substrate binding and catalysis., Berrisford JM, Akerboom J, Brouns S, Sedelnikova SE, Turnbull AP, van der Oost J, Salmon L, Hardre R, Murray IA, Blackburn GM, Rice DW, Baker PJ, J Mol Biol. 2004 Oct 22;343(3):649-57. PMID:15465052

Page seeded by OCA on Mon Jul 28 09:16:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1x82"
Personal tools