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| - | [[Image:1onx.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1onx.png|left|200px]] |
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| | {{STRUCTURE_1onx| PDB=1onx | SCENE= }} | | {{STRUCTURE_1onx| PDB=1onx | SCENE= }} |
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| - | '''crystal structure of isoaspartyl dipeptidase from escherichia coli complexed with aspartate'''
| + | ===crystal structure of isoaspartyl dipeptidase from escherichia coli complexed with aspartate=== |
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| - | ==Overview==
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| - | Isoaspartyl dipeptidase from Escherichia coli functions in protein degradation by catalyzing the hydrolysis of beta-L-isoaspartyl linkages in dipeptides. The best substrate for the enzyme reported thus far is iso-Asp-Leu. Here we report the X-ray analysis of the enzyme in its resting state and complexed with aspartate to 1.65 and 2.1 A resolution, respectively. The quaternary structure of the enzyme is octameric and can be aptly described as a tetramer of dimers. Each subunit folds into two distinct domains: the N-terminal region containing eight strands of mixed beta-sheet and the C-terminal motif that is dominated by a (beta,alpha)(8)-barrel. A binuclear zinc center is located in each subunit at the C-terminal end of the (beta,alpha)(8)-barrel. Ligands to the binuclear metal center include His 68, His 70, His 201, His 230, and Asp 285. The two zincs are bridged by a carboxylated lysine residue (Lys 162) and a solvent molecule, most likely a hydroxide ion. The product of the reaction, aspartate, binds to the enzyme by displacing the bridging solvent with its side chain functional group. From this investigation it is proposed that the reaction mechanism of the enzyme proceeds through a tetrahedral intermediate and that the bridging solvent attacks the re face of the carbonyl carbon of the scissile peptide bond. This structural analysis confirms the placement of isoaspartyl dipeptidase into the urease-related amidohydrolase superfamily.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12718528}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12718528 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12718528}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| | [[Category: Metalloprotease]] | | [[Category: Metalloprotease]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:05:05 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:07:11 2008'' |
Revision as of 11:07, 28 July 2008
Template:STRUCTURE 1onx
crystal structure of isoaspartyl dipeptidase from escherichia coli complexed with aspartate
Template:ABSTRACT PUBMED 12718528
About this Structure
1ONX is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
High-resolution X-ray structure of isoaspartyl dipeptidase from Escherichia coli., Thoden JB, Marti-Arbona R, Raushel FM, Holden HM, Biochemistry. 2003 May 6;42(17):4874-82. PMID:12718528
Page seeded by OCA on Mon Jul 28 14:07:11 2008
