1rjp: Difference between revisions

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-[[Image:1rjp.jpg|left|200px]]
+{{Seed}}
+[[Image:1rjp.png|left|200px]]
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 {{STRUCTURE_1rjp|  PDB=1rjp  |  SCENE=  }}
-'''Crystal structure of D-aminoacylase in complex with 100mM CuCl2'''
+===Crystal structure of D-aminoacylase in complex with 100mM CuCl2===
-==Overview==
+<!--
-Our structural comparison of the TIM barrel metal-dependent hydrolase(-like) superfamily suggests a classification of their divergent active sites into four types: alphabeta-binuclear, alpha-mononuclear, beta-mononuclear, and metal-independent subsets. The d-aminoacylase from Alcaligenes faecalis DA1 belongs to the beta-mononuclear subset due to the fact that the catalytically essential Zn(2+) is tightly bound at the beta site with coordination by Cys(96), His(220), and His(250), even though it possesses a binuclear active site with a weak alpha binding site. Additional Zn(2+), Cd(2+), and Cu(2+), but not Ni(2+), Co(2+), Mg(2+), Mn(2+), and Ca(2+), can inhibit enzyme activity. Crystal structures of these metal derivatives show that Zn(2+) and Cd(2+) bind at the alpha(1) subsite ligated by His(67), His(69), and Asp(366), while Cu(2+) at the alpha(2) subsite is chelated by His(67), His(69) and Cys(96). Unexpectedly, the crystal structure of the inactive H220A mutant displays that the endogenous Zn(2+) shifts to the alpha(3) subsite coordinated by His(67), His(69), Cys(96), and Asp(366), revealing that elimination of the beta site changes the coordination geometry of the alpha ion with an enhanced affinity. Kinetic studies of the metal ligand mutants such as C96D indicate the uniqueness of the unusual bridging cysteine and its involvement in catalysis. Therefore, the two metal-binding sites in the d-aminoacylase are interactive with partially mutual exclusion, thus resulting in widely different affinities for the activation/attenuation mechanism, in which the enzyme is activated by the metal ion at the beta site, but inhibited by the subsequent binding of the second ion at the alpha site.
+The line below this paragraph, {{ABSTRACT_PUBMED_14736882}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14736882 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14736882}}
 ==About this Structure==
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 ==Reference==
 The functional role of the binuclear metal center in D-aminoacylase: one-metal activation and second-metal attenuation., Lai WL, Chou LY, Ting CY, Kirby R, Tsai YC, Wang AH, Liaw SH, J Biol Chem. 2004 Apr 2;279(14):13962-7. Epub 2004 Jan 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14736882 14736882]
+Crystal structure of D-aminoacylase from Alcaligenes faecalis DA1. A novel subset of amidohydrolases and insights into the enzyme mechanism., Liaw SH, Chen SJ, Ko TP, Hsu CS, Chen CJ, Wang AH, Tsai YC, J Biol Chem. 2003 Feb 14;278(7):4957-62. Epub 2002 Nov 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12454005 12454005]
+Structural-based mutational analysis of D-aminoacylase from Alcaligenes faecalis DA1., Hsu CS, Lai WL, Chang WW, Liaw SH, Tsai YC, Protein Sci. 2002 Nov;11(11):2545-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12381838 12381838]
 [[Category: Alcaligenes faecalis]]
 [[Category: N-acyl-D-amino-acid deacylase]]
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 [[Category: Insertion]]
 [[Category: Tim barrel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 07:34:52 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:06:20 2008''