2Q09

Crystal structure of Imidazolonepropionase from environmental sample with bound inhibitor 3-(2,5-Dioxo-imidazolidin-4-yl)-propionic acid

Summary for 2Q09

• Entry DOI: 10.2210/pdb2q09/pdb
• Related: 2GOK 2OOF 2PUZ
• Descriptor: Imidazolonepropionase, FE (III) ION, 3-[(4S)-2,5-DIOXOIMIDAZOLIDIN-4-YL]PROPANOIC ACID, ... (4 entities in total)
• Functional Keywords: 9252h, nysgxrc, imidazolonepropionase, 3-(2, 5-dioxo-imidazolidin-4yl)-propionic acid, psi-2 community, structural genomics, protein structure initiative, new york sgx research center for structural genomics, hydrolase
• Biological source: unidentified
• Total number of polymer chains: 1
• Total formula weight: 45937.59

Authors

Tyagi, R.,Eswaramoorthy, S.,Burley, S.K.,Swaminathan, S.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2007-05-21, release date: 2007-06-05, Last modification date: 2024-10-30)

Primary citation

Tyagi, R.,Eswaramoorthy, S.,Burley, S.K.,Raushel, F.M.,Swaminathan, S.
A common catalytic mechanism for proteins of the HutI family.
Biochemistry, 47:5608-5615, 2008

PubMed Abstract: Imidazolonepropionase (HutI) (imidazolone-5-propanote hydrolase, EC 3.5.2.7) is a member of the amidohydrolase superfamily and catalyzes the conversion of imidazolone-5-propanoate to N-formimino-L-glutamate in the histidine degradation pathway. We have determined the three-dimensional crystal structures of HutI from Agrobacterium tumefaciens (At-HutI) and an environmental sample from the Sargasso Sea Ocean Going Survey (Es-HutI) bound to the product [ N-formimino-L-glutamate (NIG)] and an inhibitor [3-(2,5-dioxoimidazolidin-4-yl)propionic acid (DIP)], respectively. In both structures, the active site is contained within each monomer, and its organization displays the landmark feature of the amidohydrolase superfamily, showing a metal ligand (iron), four histidines, and one aspartic acid. A catalytic mechanism involving His265 is proposed on the basis of the inhibitor-bound structure. This mechanism is applicable to all HutI forms.

PubMed: 18442260
DOI: 10.1021/bi800180g

Experimental method

X-RAY DIFFRACTION (1.97 Å)