1o9p
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(New page: 200px<br /> <applet load="1o9p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o9p, resolution 1.8Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 19:22, 29 October 2007
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CRYSTAL STRUCTURE OF THE S131A MUTANT OF MALONAMIDASE E2 COMPLEXED WITH MALONATE FROM BRADYRHIZOBIUM JAPONICUM
Overview
Amidase signature family enzymes, which are widespread in nature, contain, a newly identified Ser-cisSer-Lys catalytic triad in which the peptide, bond between Ser131 and the preceding residue Gly130 is in a cis, configuration. In order to characterize the property of the novel triad, we have determined the structures of five mutant malonamidase E2 enzymes, that contain a Cys-cisSer-Lys, Ser-cisAla-Lys, or Ser-cisSer-Ala triad or, a substitution of Gly130 with alanine. Cysteine cannot replace the role of, Ser155 due to a hyper-reactivity of the residue, which results in the, modification of the cysteine to cysteinyl sulfinic acid, most likely, inside the expression host cells. The lysine residue plays a structural as, well as a catalytic role, since the substitution of the residue with, ... [(full description)]
About this Structure
1O9P is a [Single protein] structure of sequence from [Bradyrhizobium japonicum] with MLA as [ligand]. Full crystallographic information is available from [OCA].
Reference
Characterization of a novel Ser-cisSer-Lys catalytic triad in comparison with the classical Ser-His-Asp triad., Shin S, Yun YS, Koo HM, Kim YS, Choi KY, Oh BH, J Biol Chem. 2003 Jul 4;278(27):24937-43. Epub 2003 Apr 23. PMID:12711609
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