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-[[Image:2zal.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_2zal|  PDB=2zal  |  SCENE=  }}
-'''Crystal structure of E. coli isoaspartyl aminopeptidase/L-asparaginase in complex with L-aspartate'''
+===Crystal structure of E. coli isoaspartyl aminopeptidase/L-asparaginase in complex with L-aspartate===
-==Overview==
+<!--
-The crystal structure of Escherichia coli isoaspartyl aminopeptidase/asparaginase (EcAIII), an enzyme belonging to the N-terminal nucleophile (Ntn)-hydrolases family, has been determined at 1.9-A resolution for a complex obtained by cocrystallization with l-aspartate, which is a product of both enzymatic reactions catalyzed by EcAIII. The enzyme is a dimer of heterodimers, (alphabeta)(2). The (alphabeta) heterodimer, which arises by autoproteolytic cleavage of the immature protein, exhibits an alphabetabetaalpha-sandwich fold, typical for Ntn-hydrolases. The asymmetric unit contains one copy of the EcAIII.Asp complex, with clearly visible l-aspartate ligands, one bound in each of the two active sites of the enzyme. The l-aspartate ligand is located near Thr(179), the N-terminal residue of subunit beta liberated in the autoproteolytic event. Structural comparisons with the free form of EcAIII reveal that there are no major rearrangements of the active site upon aspartate binding. Although the ligand binding mode is similar to that observed in an l-aspartate complex of the related enzyme human aspartylglucosaminidase, the architecture of the EcAIII active site sheds light on the question of substrate specificity and explains why EcAIII is not able to hydrolyze glycosylated asparagine substrates.
+The line below this paragraph, {{ABSTRACT_PUBMED_15946951}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15946951 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15946951}}
 ==About this Structure==
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 ==Reference==
 Crystal structure of isoaspartyl aminopeptidase in complex with L-aspartate., Michalska K, Brzezinski K, Jaskolski M, J Biol Chem. 2005 Aug 5;280(31):28484-91. Epub 2005 Jun 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15946951 15946951]
+Crystallization and preliminary crystallographic studies of a new L-asparaginase encoded by the Escherichia coli genome., Borek D, Jaskolski M, Acta Crystallogr D Biol Crystallogr. 2000 Nov;56(Pt 11):1505-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11053866 11053866]
+A protein catalytic framework with an N-terminal nucleophile is capable of self-activation., Brannigan JA, Dodson G, Duggleby HJ, Moody PC, Smith JL, Tomchick DR, Murzin AG, Nature. 1995 Nov 23;378(6555):416-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7477383 7477383]
+Crystal structure of glycosylasparaginase from Flavobacterium meningosepticum., Xuan J, Tarentino AL, Grimwood BG, Plummer TH Jr, Cui T, Guan C, Van Roey P, Protein Sci. 1998 Mar;7(3):774-81. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9541410 9541410]
+Three-dimensional structure of human lysosomal aspartylglucosaminidase., Oinonen C, Tikkanen R, Rouvinen J, Peltonen L, Nat Struct Biol. 1995 Dec;2(12):1102-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8846222 8846222]
+Crystal structures of Flavobacterium glycosylasparaginase. An N-terminal nucleophile hydrolase activated by intramolecular proteolysis., Guo HC, Xu Q, Buckley D, Guan C, J Biol Chem. 1998 Aug 7;273(32):20205-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9685368 9685368]
+Structural insights into the mechanism of intramolecular proteolysis., Xu Q, Buckley D, Guan C, Guo HC, Cell. 1999 Sep 3;98(5):651-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10490104 10490104]
+Autoproteolytic activation of human aspartylglucosaminidase., Saarela J, Oinonen C, Jalanko A, Rouvinen J, Peltonen L, Biochem J. 2004 Mar 1;378(Pt 2):363-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14616088 14616088]
+Structure of the isoaspartyl peptidase with L-asparaginase activity from Escherichia coli., Prahl A, Pazgier M, Hejazi M, Lockau W, Lubkowski J, Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1173-6. Epub 2004, May 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15159592 15159592]
 [[Category: Escherichia coli]]
 [[Category: Protein complex]]
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 [[Category: L-aspartate/calcium cluster]]
 [[Category: Ntn-hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 20:05:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:58:37 2008''