1nvm
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(New page: 200px<br /><applet load="1nvm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nvm, resolution 1.70Å" /> '''Crystal structure of...)
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Revision as of 20:28, 20 November 2007
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Crystal structure of a bifunctional aldolase-dehydrogenase : sequestering a reactive and volatile intermediate
Overview
The crystal structure of the bifunctional enzyme 4-hydroxy-2-ketovalerate, aldolase (DmpG)/acylating acetaldehyde dehydrogenase (DmpF), which is, involved in the bacterial degradation of toxic aromatic compounds, has, been determined by multiwavelength anomalous dispersion (MAD) techniques, and refined to 1.7-A resolution. Structures of the two polypeptides, represent a previously unrecognized subclass of metal-dependent aldolases, and of a CoA-dependent dehydrogenase. The structure reveals a mixed state, of NAD+ binding to the DmpF protomer. Domain movements associated with, cofactor binding in the DmpF protomer may be correlated with channeling, and activity at the DmpG protomer. In the presence of NAD+ a 29-A-long, sequestered tunnel links the two active sites. Two barriers are visible, along the tunnel and suggest control points for the movement of the, reactive and volatile acetaldehyde intermediate between the two active, sites.
About this Structure
1NVM is a Protein complex structure of sequences from Pseudomonas sp. with MN, OXL, SO4, NAD and MPD as ligands. Active as Acetaldehyde dehydrogenase (acetylating), with EC number 1.2.1.10 Full crystallographic information is available from OCA.
Reference
Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate., Manjasetty BA, Powlowski J, Vrielink A, Proc Natl Acad Sci U S A. 2003 Jun 10;100(12):6992-7. Epub 2003 May 22. PMID:12764229
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