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.


2gq9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2gq9.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2gq9.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2gq9| PDB=2gq9 | SCENE= }}
{{STRUCTURE_2gq9| PDB=2gq9 | SCENE= }}
-
'''Structure of SYE1, an OYE homologue from S. oneidensis, in complex with p-hydroxybenzaldehyde'''
+
===Structure of SYE1, an OYE homologue from S. oneidensis, in complex with p-hydroxybenzaldehyde===
-
==Overview==
+
<!--
-
We have recently reported that Shewanella oneidensis, a Gram-negative gamma-proteobacterium with a rich arsenal of redox proteins, possesses four old yellow enzyme (OYE) homologues. Here, we report a series of high resolution crystal structures for one of these OYEs, Shewanella yellow enzyme 1 (SYE1), in its oxidized form at 1.4A resolution, which binds a molecule of PEG 400 in the active site, and in its NADH-reduced and p-hydroxybenzaldehyde- and p-hydroxyacetophenone-bound forms at 1.7A resolution. Although the overall structure of SYE1 reveals a monomeric enzyme based on the alpha(8)beta(8) barrel scaffold observed for other OYEs, the active site exhibits a unique combination of features: a strongly butterfly-bent FMN cofactor both in the oxidized and NADH-reduced forms, a collapsed and narrow active site tunnel, and a novel combination of conserved residues involved in the binding of phenolic ligands. Furthermore, we identify a second p-hydroxybenzaldehyde-binding site in a hydrophobic cleft next to the entry of the active site tunnel in the capping subdomain, formed by a restructuring of Loop 3 to an "open" conformation. This constitutes the first evidence to date for the entire family of OYEs that Loop 3 may indeed play a dynamic role in ligand binding and thus provides insights into the elusive NADH complex and into substrate binding in general. Structure-based sequence alignments indicate that the novelties we observe in SYE1 are supported by conserved residues in a number of structurally uncharacterized OYEs from the beta- and gamma-proteobacteria, suggesting that SYE1 represents a new subfamily of bacterial OYEs.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16857682}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16857682 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16857682}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Old yellow enzyme]]
[[Category: Old yellow enzyme]]
[[Category: Phenolic ligand]]
[[Category: Phenolic ligand]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:23:49 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:51:40 2008''

Revision as of 09:51, 27 July 2008

Template:STRUCTURE 2gq9

Structure of SYE1, an OYE homologue from S. oneidensis, in complex with p-hydroxybenzaldehyde

Template:ABSTRACT PUBMED 16857682

About this Structure

2GQ9 is a Single protein structure of sequence from Shewanella oneidensis. Full crystallographic information is available from OCA.

Reference

Ligand-induced conformational changes in the capping subdomain of a bacterial old yellow enzyme homologue and conserved sequence fingerprints provide new insights into substrate binding., van den Hemel D, Brige A, Savvides SN, Van Beeumen J, J Biol Chem. 2006 Sep 22;281(38):28152-61. Epub 2006 Jul 20. PMID:16857682

Page seeded by OCA on Sun Jul 27 12:51:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools