Structural highlights
3c17 is a 2 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , |
| Related: | 2zak, 1k2x, 1jn9, 2zal, 1t3m, 2gez, 9gac, 9gaf, 9gaa, 2gac |
| Gene: | ybiK (iaaA) (ECOLI) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[IAAA_ECOLI] Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Degrades L-isoaspartyl-containing di- and maybe also tripeptides. Also has L-asparaginase activity, although this may not be its principal function.[1] May be involved in glutathione, and possibly other peptide, transport, although these results could also be due to polar effects of disruption.[2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Plant l-asparaginases and their bacterial homologs, such as EcAIII found in Escherichia coli, form a subgroup of the N-terminal nucleophile (Ntn)-hydrolase family. In common with all Ntn-hydrolases, they are expressed as inactive precursors that undergo activation in an autocatalytic manner. The maturation process involves intramolecular hydrolysis of a single peptide bond, leading to the formation of two subunits (alpha and beta) folded as one structural domain, with the nucleophilic Thr residue located at the freed N terminus of subunit beta. The mechanism of the autocleavage reaction remains obscure. We have determined the crystal structure of an active site mutant of EcAIII, with the catalytic Thr residue substituted by Ala (T179A). The modification has led to a correctly folded but unprocessed molecule, revealing the geometry and molecular environment of the scissile peptide bond. The autocatalytic reaction is analyzed from the point of view of the Thr(179) side chain rotation, identification of a potential general base residue, and the architecture of the oxyanion hole.
The mechanism of autocatalytic activation of plant-type L-asparaginases.,Michalska K, Hernandez-Santoyo A, Jaskolski M J Biol Chem. 2008 May 9;283(19):13388-97. Epub 2008 Mar 10. PMID:18334484[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hejazi M, Piotukh K, Mattow J, Deutzmann R, Volkmer-Engert R, Lockau W. Isoaspartyl dipeptidase activity of plant-type asparaginases. Biochem J. 2002 May 15;364(Pt 1):129-36. PMID:11988085
- ↑ Hejazi M, Piotukh K, Mattow J, Deutzmann R, Volkmer-Engert R, Lockau W. Isoaspartyl dipeptidase activity of plant-type asparaginases. Biochem J. 2002 May 15;364(Pt 1):129-36. PMID:11988085
- ↑ Michalska K, Hernandez-Santoyo A, Jaskolski M. The mechanism of autocatalytic activation of plant-type L-asparaginases. J Biol Chem. 2008 May 9;283(19):13388-97. Epub 2008 Mar 10. PMID:18334484 doi:10.1074/jbc.M800746200
