2hp3
From Proteopedia
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'''Crystal structure of iminodisuccinate epimerase''' | '''Crystal structure of iminodisuccinate epimerase''' | ||
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[[Category: Schneider, G.]] | [[Category: Schneider, G.]] | ||
[[Category: 6 helix bundle]] | [[Category: 6 helix bundle]] | ||
| - | [[Category: | + | [[Category: Chorismate mutase like]] |
| - | [[Category: | + | [[Category: Mmge/prpd fold]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:32:09 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:32, 4 May 2008
Crystal structure of iminodisuccinate epimerase
Overview
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.
About this Structure
2HP3 is a Single protein structure of sequence from Agrobacterium tumefaciens. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of iminodisuccinate epimerase defines the fold of the MmgE/PrpD protein family., Lohkamp B, Bauerle B, Rieger PG, Schneider G, J Mol Biol. 2006 Sep 22;362(3):555-66. Epub 2006 Jul 29. PMID:16934291 Page seeded by OCA on Sun May 4 06:32:09 2008
