2hp0: Difference between revisions

Revision as of 18:44, 21 February 2008

Crystal structure of iminodisuccinate epimerase

OverviewOverview

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 StructureAbout this Structure

2HP0 is a Protein complex structure of sequences from Agrobacterium tumefaciens with , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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 Thu Feb 21 17:44:06 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 15: / Line 15: @@
 [[Category: Bauerle, B.]]
 [[Category: Lohkamp, B.]]
-[[Category: Rieger, P.G.]]
+[[Category: Rieger, P G.]]
 [[Category: Schneider, G.]]
 [[Category: DTT]]
@@ Line 24: / Line 24: @@
 [[Category: mmge/prpd fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:25:48 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:44:06 2008''