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2q09
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'''Crystal structure of Imidazolonepropionase from environmental sample with bound inhibitor 3-(2,5-Dioxo-imidazolidin-4-yl)-propionic acid''' | '''Crystal structure of Imidazolonepropionase from environmental sample with bound inhibitor 3-(2,5-Dioxo-imidazolidin-4-yl)-propionic acid''' | ||
| + | |||
| + | ==Overview== | ||
| + | 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. | ||
==About this Structure== | ==About this Structure== | ||
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q09 OCA]. | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q09 OCA]. | ||
| + | |||
| + | ==Reference== | ||
| + | A common catalytic mechanism for proteins of the HutI family., Tyagi R, Eswaramoorthy S, Burley SK, Raushel FM, Swaminathan S, Biochemistry. 2008 May 20;47(20):5608-15. Epub 2008 Apr 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18442260 18442260] | ||
[[Category: Imidazolonepropionase]] | [[Category: Imidazolonepropionase]] | ||
[[Category: Burley, S K.]] | [[Category: Burley, S K.]] | ||
[[Category: Eswaramoorthy, S.]] | [[Category: Eswaramoorthy, S.]] | ||
| - | [[Category: NYSGXRC, New York | + | [[Category: NYSGXRC, New York SGX Research Center for Structural Genomics.]] |
[[Category: Swaminathan, S.]] | [[Category: Swaminathan, S.]] | ||
[[Category: Tyagi, R.]] | [[Category: Tyagi, R.]] | ||
[[Category: 9252h]] | [[Category: 9252h]] | ||
| + | [[Category: Hydrolase]] | ||
[[Category: Imidazolonepropionase]] | [[Category: Imidazolonepropionase]] | ||
| - | [[Category: New york | + | [[Category: New york sgx research center for structural genomic]] |
[[Category: Nysgxrc]] | [[Category: Nysgxrc]] | ||
[[Category: Protein structure initiative]] | [[Category: Protein structure initiative]] | ||
| - | [[Category: | + | [[Category: Psi-2 community]] |
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:17:15 2008'' |
Revision as of 09:17, 18 June 2008
Crystal structure of Imidazolonepropionase from environmental sample with bound inhibitor 3-(2,5-Dioxo-imidazolidin-4-yl)-propionic acid
Overview
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.
About this Structure
Full crystallographic information is available from OCA.
Reference
A common catalytic mechanism for proteins of the HutI family., Tyagi R, Eswaramoorthy S, Burley SK, Raushel FM, Swaminathan S, Biochemistry. 2008 May 20;47(20):5608-15. Epub 2008 Apr 29. PMID:18442260 Page seeded by OCA on Wed Jun 18 12:17:15 2008
Categories: Imidazolonepropionase | Burley, S K. | Eswaramoorthy, S. | NYSGXRC, New York SGX Research Center for Structural Genomics. | Swaminathan, S. | Tyagi, R. | 9252h | Hydrolase | New york sgx research center for structural genomic | Nysgxrc | Protein structure initiative | Psi-2 community | Structural genomic
