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| - | [[Image:2bb0.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2bb0| PDB=2bb0 | SCENE= }} | | {{STRUCTURE_2bb0| PDB=2bb0 | SCENE= }} |
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| - | '''Structure of Imidazolonepropionase from Bacillus subtilis'''
| + | ===Structure of Imidazolonepropionase from Bacillus subtilis=== |
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| - | ==Overview==
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| - | Imidazolonepropionase (EC 3.5.2.7) catalyzes the third step in the universal histidine degradation pathway, hydrolyzing the carbon-nitrogen bonds in 4-imidazolone-5-propionic acid to yield N-formimino-l-glutamic acid. Here we report the crystal structures of the Bacillus subtilis imidazolonepropionase and its complex at 2.0-A resolution with substrate analog imidazole-4-acetic acid sodium (I4AA). The structure of the native enzyme contains two domains, a TIM (triose-phosphate isomerase) barrel domain with two insertions and a small beta-sandwich domain. The TIM barrel domain is quite similar to the members of the alpha/beta barrel metallo-dependent hydrolase superfamily, especially to Escherichia coli cytosine deaminase. A metal ion was found in the central cavity of the TIM barrel and was tightly coordinated to residues His-80, His-82, His-249, Asp-324, and a water molecule. X-ray fluorescence scan analysis confirmed that the bound metal ion was a zinc ion. An acetate ion, 6 A away from the zinc ion, was also found in the potential active site. In the complex structure with I4AA, a substrate analog, I4AA replaced the acetate ion and contacted with Arg-89, Try-102, Tyr-152, His-185, and Glu-252, further defining and confirming the active site. The detailed structural studies allowed us to propose a zinc-activated nucleophilic attack mechanism for the hydrolysis reaction catalyzed by the enzyme.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16990261}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16990261 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16990261}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| | [[Category: Tim barrel]] | | [[Category: Tim barrel]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:14:19 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:41:23 2008'' |
Revision as of 13:41, 27 July 2008
Template:STRUCTURE 2bb0
Structure of Imidazolonepropionase from Bacillus subtilis
Template:ABSTRACT PUBMED 16990261
About this Structure
2BB0 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
A catalytic mechanism revealed by the crystal structures of the imidazolonepropionase from Bacillus subtilis., Yu Y, Liang YH, Brostromer E, Quan JM, Panjikar S, Dong YH, Su XD, J Biol Chem. 2006 Dec 1;281(48):36929-36. Epub 2006 Sep 21. PMID:16990261
Page seeded by OCA on Sun Jul 27 16:41:23 2008
