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| {{STRUCTURE_2hp0| PDB=2hp0 | SCENE= }} | | {{STRUCTURE_2hp0| PDB=2hp0 | SCENE= }} |
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| '''Crystal structure of iminodisuccinate epimerase'''
| | ===Crystal structure of iminodisuccinate epimerase=== |
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| ==Overview==
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| Iminodisuccinate (IDS) epimerase catalyzes the epimerisation of R,R-, S,S- and R,S- iminodisuccinate, one step in the biodegradation of the chelating agent iminodisuccinate by Agrobacterium tumefaciens BY6. The enzyme is a member of the MmgE/PrpD protein family, a diverse and little characterized class of proteins of prokaryotic and eukaryotic origin. IDS epimerase does not show significant overall amino acid sequence similarity to any other protein of known three-dimensional structure. The crystal structure of this novel epimerase has been determined by multi-wavelength diffraction to 1.5 A resolution using selenomethionine-substituted enzyme. In the crystal, the enzyme forms a homo-dimer, and the subunit consists of two domains. The larger domain, not consecutive in sequence and comprising residues Met1-Lys266 and Leu400-Pro446, forms a novel all alpha-helical fold with a central six-helical bundle. The second, smaller domain folds into an alpha+beta domain, related in topology to chorismate mutase by a circular permutation. IDS epimerase is thus not related in three-dimensional structure to other known epimerases. The fold of the IDS epimerase is representative for the whole MmgE/PrpD family. The putative active site is located at the interface between the two domains of the subunit, and is characterized by a positively charged surface, consistent with the binding of a highly negatively charged substrate such as iminodisuccinate. Docking experiments suggest a two-base mechanism for the epimerisation reaction.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16934291}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16934291 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16934291}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Chorismate mutase like]] | | [[Category: Chorismate mutase like]] |
| [[Category: Mmge/prpd fold]] | | [[Category: Mmge/prpd fold]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:32:04 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:19:37 2008'' |
