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| - | [[Image:2gou.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2gou| PDB=2gou | SCENE= }} | | {{STRUCTURE_2gou| PDB=2gou | SCENE= }} |
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| - | '''Structure of wild type, oxidized SYE1, an OYE homologue from S. oneidensis'''
| + | ===Structure of wild type, oxidized 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: Fmn]] | | [[Category: Fmn]] |
| | [[Category: Old yeallow enzyme]] | | [[Category: Old yeallow enzyme]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:20:52 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:09:00 2008'' |
Revision as of 16:09, 28 July 2008
Template:STRUCTURE 2gou
Structure of wild type, oxidized SYE1, an OYE homologue from S. oneidensis
Template:ABSTRACT PUBMED 16857682
About this Structure
2GOU 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
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