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| - | [[Image:1nfg.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1nfg| PDB=1nfg | SCENE= }} | | {{STRUCTURE_1nfg| PDB=1nfg | SCENE= }} |
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| - | '''Structure of D-hydantoinase'''
| + | ===Structure of D-hydantoinase=== |
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| - | ==Overview==
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| - | D-Hydantoinase (D-HYD) is an industrial enzyme that is widely used in the production of D-amino acids which are precursors for semisynthesis of antibiotics, peptides, and pesticides. This report describes the crystal structure of D-hydantoinase from Burkholderia pickettii (HYD(Bp)) at a 2.7-A resolution. The structure of HYD(Bp) consists of a core (alpha/beta)(8) triose phosphate isomerase barrel fold and a beta-sheet domain, and the catalytic active site consists of two metal ions and six highly conserved amino acid residues. Although HYD(Bp) shares only moderate sequence similarity with D-HYDs from Thermus sp. (HYD(Tsp)) and Bacillus stearothermophilus (HYD(Bst)), whose structures have recently been solved, the overall structure and the structure of the catalytic active site are strikingly similar. Nevertheless, the amino acids that compose the substrate-binding site are less conserved and have different properties, which might dictate the substrate specificity. Structural comparison has revealed insights into the molecular basis of the differential thermostability of D-HYDs. The more thermostable HYD(Tsp) contains more aromatic residues in the interior of the structure than HYD(Bp) and HYD(Bst). Changes of large aromatic residues in HYD(Tsp) to smaller residues in HYD(Bp) or HYD(Bst) decrease the hydrophobicity and create cavities inside the structure. HYD(Tsp) has more salt bridges and hydrogen-bonding interactions and less oxidation susceptible Met and Cys residues on the protein surface than HYD(Bp) and HYD(Bst). Besides, HYD(Tsp) also contains more rigid Pro residues. These factors are likely to make major contributions to the varying thermostability of these enzymes. This information could be exploited in helping to engineer more thermostable mesophilic enzymes.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12837777}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12837777 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12837777}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Yang, Y.]] | | [[Category: Yang, Y.]] |
| | [[Category: Tim barrel]] | | [[Category: Tim barrel]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:28:12 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:11:57 2008'' |
Revision as of 18:11, 27 July 2008
Template:STRUCTURE 1nfg
Structure of D-hydantoinase
Template:ABSTRACT PUBMED 12837777
About this Structure
1NFG is a Single protein structure of sequence from Ralstonia pickettii. Full crystallographic information is available from OCA.
Reference
Crystal structure of D-Hydantoinase from Burkholderia pickettii at a resolution of 2.7 Angstroms: insights into the molecular basis of enzyme thermostability., Xu Z, Liu Y, Yang Y, Jiang W, Arnold E, Ding J, J Bacteriol. 2003 Jul;185(14):4038-49. PMID:12837777
Page seeded by OCA on Sun Jul 27 21:11:57 2008
