2VLB

Structure of unliganded arylmalonate decarboxylase

Summary for 2VLB

• Entry DOI: 10.2210/pdb2vlb/pdb
• Descriptor: ARYLMALONATE DECARBOXYLASE, BETA-MERCAPTOETHANOL, PHOSPHATE ION, ... (5 entities in total)
• Functional Keywords: protein dynamics, lyase, amdase, decarboxylase, decarboxylation
• Biological source: BORDETELLA BRONCHISEPTICA
• Total number of polymer chains: 4
• Total formula weight: 105420.54

Authors

Kuettner, E.B.,Keim, A.,Kircher, M.,Rosmus, S.,Strater, N. (deposition date: 2008-01-11, release date: 2008-03-18, Last modification date: 2019-05-29)

Primary citation

Kuettner, E.B.,Keim, A.,Kircher, M.,Rosmus, S.,Strater, N.
Active Site Mobility Revealed by the Crystal Structure of Arylmalonate Decarboxylase from Bordetella Bronchiseptica
J.Mol.Biol., 377:386-, 2008

PubMed Abstract: 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.

PubMed: 18258259
DOI: 10.1016/J.JMB.2007.12.069

Experimental method

X-RAY DIFFRACTION (1.92 Å)