2hp0: Difference between revisions
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|PDB= 2hp0 |SIZE=350|CAPTION= <scene name='initialview01'>2hp0</scene>, resolution 1.50Å | |PDB= 2hp0 |SIZE=350|CAPTION= <scene name='initialview01'>2hp0</scene>, resolution 1.50Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= ite ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=358 Agrobacterium tumefaciens]) | |GENE= ite ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=358 Agrobacterium tumefaciens]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hp0 OCA], [http://www.ebi.ac.uk/pdbsum/2hp0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hp0 RCSB]</span> | |||
}} | }} | ||
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[[Category: Rieger, P G.]] | [[Category: Rieger, P G.]] | ||
[[Category: Schneider, G.]] | [[Category: Schneider, G.]] | ||
[[Category: 6 helix bundle]] | [[Category: 6 helix bundle]] | ||
[[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 | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:33:19 2008'' | ||
Revision as of 03:33, 31 March 2008
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| , resolution 1.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Gene: | ite (Agrobacterium tumefaciens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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