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Product Summary
Fragment
Full length
Protein Description
Enolase-phosphatase E1
Background
Enolase-phosphatase E1 (MASA) is a bifunctional enzyme in the ubiquitous methionine salvage pathway that catalyzes the continuous reactions of 2,3-diketo-5-methylthio-1-phosphopentane to yield the aci-reductone metabolite using Mg2+ as cofactor. In this study, we have determined the crystal structure of MASA and its complex with a substrate analog to 1.7A resolution by multi-wavelength anomalous diffraction and molecular replacement techniques, respectively.
Protein Classification
Hydrolase
Structure Weight
29316.11 Da
PDBID
1ZS9
Method
X-Ray Diffraction
Resolution
1.7Å
Ligand Chemical Component
Selenomethionine
Reference
Wang, H., Pang, H., Bartlam, M., Rao, Z. (2005) Crystal Structure of Human E1 Enzyme and its Complex with a Substrate Analog Reveals the Mechanism of its Phosphatase/Enolase J.Mol.Biol. 348: 917-926
cDNALength
855