7VDY

Crystal structure of O-ureidoserine racemase

Summary for 7VDY

• Entry DOI: 10.2210/pdb7vdy/pdb
• Descriptor: O-ureido-serine racemase, SULFATE ION (3 entities in total)
• Functional Keywords: racemase, isomerase
• Biological source: Streptomyces lavendulae
• Total number of polymer chains: 2
• Total formula weight: 63943.75

Authors

Oda, K.,Matoba, Y. (deposition date: 2021-09-07, release date: 2021-12-15, Last modification date: 2023-11-29)

Primary citation

Oda, K.,Sakaguchi, T.,Matoba, Y.
Crystal structure of O-ureidoserine racemase found in the d-cycloserine biosynthetic pathway.
Proteins, 90:912-918, 2022

PubMed Abstract: The O-ureidoserine racemase (DcsC) is an enzyme found from the biosynthetic gene cluster of antitubercular agent d-cycloserine. Although DcsC is homologous to diaminopimelate epimerase (DapF) that catalyzes the interconversion between ll- and dl-diaminopimelic acid, it specifically catalyzes the interconversion between O-ureido-l-serine and its enantiomer. Here we determined the crystal structure of DcsC at a resolution of 2.12 Å, implicating that the catalytic mechanism of DcsC shares similarity with that of DapF. Comparing the structure of the active center of DcsC to that of DapF, Thr72, Thr198, and Tyr219 of DcsC are likely to be involved in the substrate specificity.

PubMed: 34877716
DOI: 10.1002/prot.26290

Experimental method

X-RAY DIFFRACTION (2.12 Å)