2vlb
From Proteopedia
| |||||||
| , resolution 1.92Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , , , , , , , , , and | ||||||
| Ligands: | , , | ||||||
| Activity: | Arylmalonate decarboxylase, with EC number 4.1.1.76 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF UNLIGANDED ARYLMALONATE DECARBOXYLASE
Overview
Arylmalonate decarboxylase (AMDase) from Bordetella bronchiseptica catalyzes the enantioselective decarboxylation of arylmethylmalonates without the need for an organic cofactor or metal ion. The decarboxylation reaction is of interest for the synthesis of fine chemicals. As basis for an analysis of the catalytic mechanism of AMDase and for a rational enzyme design, we determined the X-ray structure of the enzyme up to 1.9 A resolution. Like the distantly related aspartate or glutamate racemases, AMDase has an aspartate transcarbamoylase fold consisting of two alpha/beta domains related by a pseudo dyad. However, the domain orientation of AMDase differs by about 30 degrees from that of the glutamate racemases, and also significant differences in active-site structures are observed. In the crystals, four independent subunits showing different conformations of active-site loops are present. This finding is likely to reflect the active-site mobility necessary for catalytic activity.
About this Structure
2VLB is a Single protein structure of sequence from Bordetella bronchiseptica. Full crystallographic information is available from OCA.
Reference
Active-site mobility revealed by the crystal structure of arylmalonate decarboxylase from Bordetella bronchiseptica., Kuettner EB, Keim A, Kircher M, Rosmus S, Strater N, J Mol Biol. 2008 Mar 21;377(2):386-94. Epub 2008 Jan 5. PMID:18258259
Page seeded by OCA on Mon Mar 31 05:13:28 2008
