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| {{STRUCTURE_2gqa| PDB=2gqa | SCENE= }} | | {{STRUCTURE_2gqa| PDB=2gqa | SCENE= }} |
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| '''Structure of NADH-reduced SYE1, an OYE homologue from S. oneidensis'''
| | ===Structure of NADH-reduced SYE1, an OYE homologue from S. oneidensis=== |
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| ==Overview==
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| 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. |
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| | {{ABSTRACT_PUBMED_16857682}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Old yellow enzyme]] | | [[Category: Old yellow enzyme]] |
| [[Category: Reduction by nadh]] | | [[Category: Reduction by nadh]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:23:55 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:18:29 2008'' |