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2zak

From Proteopedia

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Revision as of 04:03, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

Image:2zak.png

Template:STRUCTURE 2zak

Orthorhombic crystal structure of precursor E. coli isoaspartyl peptidase/L-asparaginase (EcAIII) with active-site T179A mutation

Template:ABSTRACT PUBMED 18323626

About this Structure

2ZAK is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal packing of plant-type L-asparaginase from Escherichia coli., Michalska K, Borek D, Hernandez-Santoyo A, Jaskolski M, Acta Crystallogr D Biol Crystallogr. 2008 Mar;64(Pt 3):309-20. Epub 2008, Feb 20. PMID:18323626

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

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

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

Page seeded by OCA on Mon Jul 28 07:03:09 2008

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OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2zak"

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-[[Image:2zak.jpg|left|200px]]
+{{Seed}}
+[[Image:2zak.png|left|200px]]
 <!--
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 {{STRUCTURE_2zak|  PDB=2zak  |  SCENE=  }}
-'''Orthorhombic crystal structure of precursor E. coli isoaspartyl peptidase/L-asparaginase (EcAIII) with active-site T179A mutation'''
+===Orthorhombic crystal structure of precursor E. coli isoaspartyl peptidase/L-asparaginase (EcAIII) with active-site T179A mutation===
-==Overview==
+<!--
-Plant-type L-asparaginases hydrolyze the side-chain amide bond of L-asparagine or its beta-peptides. They belong to the N-terminal nucleophile (Ntn) hydrolases and are synthesized as inactive precursor molecules. Activation occurs via the autoproteolytic release of two subunits, alpha and beta, the latter of which carries the nucleophile at its N-terminus. Crystallographic studies of plant-type asparaginases have focused on an Escherichia coli homologue (EcAIII), which has been crystallized in several crystal forms. Although they all belong to the same P2(1)2(1)2(1) space group with similar unit-cell parameters, they display different crystal-packing arrangements and thus should be classified as separate polymorphs. This variability stems mainly from different positions of the EcAIII molecules within the unit cell, although they also exhibit slight differences in orientation. The intermolecular interactions that trigger different crystal lattice formation are mediated by ions, which represent the most variable component of the crystallization conditions. This behaviour confirms recent observations that small molecules might promote protein crystal lattice formation.
+The line below this paragraph, {{ABSTRACT_PUBMED_18323626}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18323626 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18323626}}
 ==About this Structure==
@@ Line 20: / Line 24: @@
 ==Reference==
 Crystal packing of plant-type L-asparaginase from Escherichia coli., Michalska K, Borek D, Hernandez-Santoyo A, Jaskolski M, Acta Crystallogr D Biol Crystallogr. 2008 Mar;64(Pt 3):309-20. Epub 2008, Feb 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18323626 18323626]
+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]
+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]
+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]
+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]
+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]
+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]
+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]
+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]
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
@@ Line 30: / Line 52: @@
 [[Category: Ntn-hydrolase]]
 [[Category: Precursor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 20:05:44 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:03:09 2008''

2zak

From Proteopedia

Revision as of 04:03, 28 July 2008

Orthorhombic crystal structure of precursor E. coli isoaspartyl peptidase/L-asparaginase (EcAIII) with active-site T179A mutation

About this Structure

Reference

Proteopedia Page Contributors and Editors (what is this?)

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