We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1al7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1al7.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1al7.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1al7| PDB=1al7 | SCENE= }}
{{STRUCTURE_1al7| PDB=1al7 | SCENE= }}
-
'''THREE-DIMENSIONAL STRUCTURES OF GLYCOLATE OXIDASE WITH BOUND ACTIVE-SITE INHIBITORS'''
+
===THREE-DIMENSIONAL STRUCTURES OF GLYCOLATE OXIDASE WITH BOUND ACTIVE-SITE INHIBITORS===
-
==Overview==
+
<!--
-
A key step in plant photorespiration, the oxidation of glycolate to glyoxylate, is carried out by the peroxisomal flavoprotein glycolate oxidase (EC 1.1.3.15). The three-dimensional structure of this alpha/beta barrel protein has been refined to 2 A resolution (Lindqvist Y. 1989. J Mol Biol 209:151-166). FMN dependent glycolate oxidase is a member of the family of alpha-hydroxy acid oxidases. Here we describe the crystallization and structure determination of two inhibitor complexes of the enzyme, TKP (3-Decyl-2,5-dioxo-4-hydroxy-3-pyrroline) and TACA (4-Carboxy-5-(1-pentyl)hexylsulfanyl-1,2,3-triazole). The structure of the TACA complex has been refined to 2.6 A resolution and the TKP complex, solved with molecular replacement, to 2.2 A resolution. The Rfree for the TACA and TKP complexes are 24.2 and 25.1%, respectively. The overall structures are very similar to the unliganded holoenzyme, but a closer examination of the active site reveals differences in the positioning of the flavin isoalloxazine ring and a displaced flexible loop in the TKP complex. The two inhibitors differ in binding mode and hydrophobic interactions, and these differences are reflected by the very different Ki values for the inhibitors, 16 nM for TACA and 4.8 microM for TKP. Implications of the structures of these enzyme-inhibitor complexes for the model for substrate binding and catalysis proposed from the holo-enzyme structure are discussed.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9144771}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9144771 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9144771}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Flavoprotein]]
[[Category: Flavoprotein]]
[[Category: Inhibitor binding]]
[[Category: Inhibitor binding]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:24:58 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:04:52 2008''

Revision as of 14:04, 30 June 2008

Image:1al7.png

Template:STRUCTURE 1al7

THREE-DIMENSIONAL STRUCTURES OF GLYCOLATE OXIDASE WITH BOUND ACTIVE-SITE INHIBITORS

Template:ABSTRACT PUBMED 9144771

About this Structure

1AL7 is a Single protein structure of sequence from Spinacia oleracea. Full crystallographic information is available from OCA.

Reference

Three-dimensional structures of glycolate oxidase with bound active-site inhibitors., Stenberg K, Lindqvist Y, Protein Sci. 1997 May;6(5):1009-15. PMID:9144771

Page seeded by OCA on Mon Jun 30 17:04:52 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1al7"
Personal tools