1NVM

Crystal structure of a bifunctional aldolase-dehydrogenase : sequestering a reactive and volatile intermediate

Summary for 1NVM

• Entry DOI: 10.2210/pdb1nvm/pdb
• Descriptor: 4-hydroxy-2-oxovalerate aldolase, acetaldehyde dehydrogenase (acylating), MANGANESE (II) ION, ... (8 entities in total)
• Functional Keywords: sequestered tunnel, substrate channeling, bifunctional enzyme, lyase-oxidoreductase complex, lyase/oxidoreductase
• Biological source: Pseudomonas sp.; More
• Total number of polymer chains: 8
• Total formula weight: 285361.73

Authors

Manjasetty, A.B.,Powlowski, J.,Vrielink, A. (deposition date: 2003-02-04, release date: 2003-06-17, Last modification date: 2024-02-14)

Primary citation

Manjasetty, A.B.,Powlowski, J.,Vrielink, A.
Crystal structure of a bifunctional aldolase-dehydrogenase: Sequestering a reactive and volatile intermediate
Proc.Natl.Acad.Sci.USA, 100:6992-6997, 2003

PubMed Abstract: 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.

PubMed: 12764229
DOI: 10.1073/pnas.1236794100

Experimental method

X-RAY DIFFRACTION (1.7 Å)