2hp0: Difference between revisions
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[[Image:2hp0.gif|left|200px]] | [[Image:2hp0.gif|left|200px]] | ||
'''Crystal structure of iminodisuccinate epimerase''' | {{Structure | ||
|PDB= 2hp0 |SIZE=350|CAPTION= <scene name='initialview01'>2hp0</scene>, resolution 1.50Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene> and <scene name='pdbligand=UNX:UNKNOWN ATOM OR ION'>UNX</scene> | |||
|ACTIVITY= | |||
|GENE= ite ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=358 Agrobacterium tumefaciens]) | |||
}} | |||
'''Crystal structure of iminodisuccinate epimerase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2HP0 is a [ | 2HP0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HP0 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16934291 16934291] | ||
[[Category: Agrobacterium tumefaciens]] | [[Category: Agrobacterium tumefaciens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: mmge/prpd fold]] | [[Category: mmge/prpd fold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:19:43 2008'' | ||
Revision as of 18:19, 20 March 2008
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| , resolution 1.50Å | |||||||
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| Ligands: | , and | ||||||
| Gene: | ite (Agrobacterium tumefaciens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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