2hp3: Difference between revisions

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[[Image:2hp3.jpg|left|200px]]
[[Image:2hp3.jpg|left|200px]]


{{Structure
<!--
|PDB= 2hp3 |SIZE=350|CAPTION= <scene name='initialview01'>2hp3</scene>, resolution 1.71&Aring;
The line below this paragraph, containing "STRUCTURE_2hp3", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>
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|ACTIVITY=
or leave the SCENE parameter empty for the default display.
|GENE= ite ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=358 Agrobacterium tumefaciens])
-->
|DOMAIN=
{{STRUCTURE_2hp3| PDB=2hp3  | SCENE= }}  
|RELATEDENTRY=[[2hp0|2HP0]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hp3 OCA], [http://www.ebi.ac.uk/pdbsum/2hp3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hp3 RCSB]</span>
}}


'''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: chorismate mutase like]]
[[Category: Chorismate mutase like]]
[[Category: mmge/prpd fold]]
[[Category: Mmge/prpd fold]]
 
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Revision as of 06:32, 4 May 2008

File:2hp3.jpg

Template:STRUCTURE 2hp3

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

2HP3 is a Single protein structure of sequence 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 Page seeded by OCA on Sun May 4 06:32:09 2008

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