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3c17

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{{STRUCTURE_3c17| PDB=3c17 | SCENE= }}
{{STRUCTURE_3c17| PDB=3c17 | SCENE= }}
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'''Hexagonal Crystal Structure of Precursor E. coli Isoaspartyl Peptidase/l-Asparaginase (ECAIII) with Active-site T179A mutation'''
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===Hexagonal Crystal Structure of Precursor E. coli Isoaspartyl Peptidase/l-Asparaginase (ECAIII) with Active-site T179A mutation===
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==Overview==
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Plant L-asparaginases and their bacterial homologs, such as EcAIII found in E. coli, form a subgroup of the 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 Thr179 side chain rotation, identification of a potential general-base residue, and the architecture of the oxyanion hole.
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(as it appears on PubMed at http://www.pubmed.gov), where 18334484 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18334484}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
The mechanism of autocatalytic activation of plant-type L-asparaginases., Michalska K, Hernandez-Santoyo A, Jaskolski M, J Biol Chem. 2008 Mar 10;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18334484 18334484]
The mechanism of autocatalytic activation of plant-type L-asparaginases., Michalska K, Hernandez-Santoyo A, Jaskolski M, J Biol Chem. 2008 Mar 10;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18334484 18334484]
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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]
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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]
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Crystal structure of plant asparaginase., Michalska K, Bujacz G, Jaskolski M, J Mol Biol. 2006 Jun 30;360(1):105-16. Epub 2006 May 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16725155 16725155]
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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]
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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]
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Characterization and functional analysis of the cis-autoproteolysis active center of glycosylasparaginase., Guan C, Liu Y, Shao Y, Cui T, Liao W, Ewel A, Whitaker R, Paulus H, J Biol Chem. 1998 Apr 17;273(16):9695-702. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9545304 9545304]
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Activation and oligomerization of aspartylglucosaminidase., Saarela J, Laine M, Tikkanen R, Oinonen C, Jalanko A, Rouvinen J, Peltonen L, J Biol Chem. 1998 Sep 25;273(39):25320-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9737998 9737998]
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A dual role for an aspartic acid in glycosylasparaginase autoproteolysis., Qian X, Guan C, Guo HC, Structure. 2003 Aug;11(8):997-1003. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12906830 12906830]
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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]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Ntn-hydrolase]]
[[Category: Ntn-hydrolase]]
[[Category: Precursor]]
[[Category: Precursor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 21:16:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:50:06 2008''

Revision as of 10:50, 27 July 2008

Image:3c17.png

Template:STRUCTURE 3c17

Hexagonal Crystal Structure of Precursor E. coli Isoaspartyl Peptidase/l-Asparaginase (ECAIII) with Active-site T179A mutation

Template:ABSTRACT PUBMED 18334484

About this Structure

3C17 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The mechanism of autocatalytic activation of plant-type L-asparaginases., Michalska K, Hernandez-Santoyo A, Jaskolski M, J Biol Chem. 2008 Mar 10;. PMID:18334484

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: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:11053866

Crystal structure of plant asparaginase., Michalska K, Bujacz G, Jaskolski M, J Mol Biol. 2006 Jun 30;360(1):105-16. Epub 2006 May 15. PMID:16725155

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:15159592

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:10490104

Characterization and functional analysis of the cis-autoproteolysis active center of glycosylasparaginase., Guan C, Liu Y, Shao Y, Cui T, Liao W, Ewel A, Whitaker R, Paulus H, J Biol Chem. 1998 Apr 17;273(16):9695-702. PMID:9545304

Activation and oligomerization of aspartylglucosaminidase., Saarela J, Laine M, Tikkanen R, Oinonen C, Jalanko A, Rouvinen J, Peltonen L, J Biol Chem. 1998 Sep 25;273(39):25320-8. PMID:9737998

A dual role for an aspartic acid in glycosylasparaginase autoproteolysis., Qian X, Guan C, Guo HC, Structure. 2003 Aug;11(8):997-1003. PMID:12906830

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:7477383

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