2GQ8

Structure of SYE1, an OYE homologue from S. ondeidensis, in complex with p-hydroxyacetophenone

Summary for 2GQ8

• Entry DOI: 10.2210/pdb2gq8/pdb
• Related: 2gou 2gq9 2gqa
• Descriptor: oxidoreductase, FMN-binding, octyl beta-D-glucopyranoside, SULFATE ION, ... (7 entities in total)
• Functional Keywords: old yellow enzyme, flavoenzyme, fmn, phenolic ligands, oxidoreductase
• Biological source: Shewanella oneidensis
• Total number of polymer chains: 1
• Total formula weight: 40734.65

Authors

Savvides, S.N.,van den Hemel, D. (deposition date: 2006-04-20, release date: 2006-07-25, Last modification date: 2024-02-14)

Primary citation

van den Hemel, D.,Brige, A.,Savvides, S.N.,Van Beeumen, J.
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.
J.Biol.Chem., 281:28152-28161, 2006

PubMed Abstract: 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.

PubMed: 16857682
DOI: 10.1074/jbc.M603946200

Experimental method

X-RAY DIFFRACTION (1.7 Å)