2zak

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{{Seed}}
 
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[[Image:2zak.png|left|200px]]
 
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==Orthorhombic crystal structure of precursor E. coli isoaspartyl peptidase/L-asparaginase (EcAIII) with active-site T179A mutation==
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The line below this paragraph, containing "STRUCTURE_2zak", creates the "Structure Box" on the page.
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<StructureSection load='2zak' size='340' side='right'caption='[[2zak]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2zak]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZAK FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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{{STRUCTURE_2zak| PDB=2zak | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zak OCA], [https://pdbe.org/2zak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zak RCSB], [https://www.ebi.ac.uk/pdbsum/2zak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zak ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IAAA_ECOLI IAAA_ECOLI] Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Degrades L-isoaspartyl-containing di- and maybe also tripeptides. Also has L-asparaginase activity, although this may not be its principal function.<ref>PMID:11988085</ref> May be involved in glutathione, and possibly other peptide, transport, although these results could also be due to polar effects of disruption.<ref>PMID:11988085</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/za/2zak_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2zak ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Orthorhombic crystal structure of precursor E. coli isoaspartyl peptidase/L-asparaginase (EcAIII) with active-site T179A mutation===
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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<ref>PMID:18323626</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2zak" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18323626}}, adds the Publication Abstract to the page
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*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18323626 is the PubMed ID number.
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*[[Asparaginase 3D structures|Asparaginase 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_18323626}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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2ZAK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZAK OCA].
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[[Category: Escherichia coli K-12]]
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[[Category: Large Structures]]
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==Reference==
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[[Category: Hernandez-Santoyo A]]
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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]
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[[Category: Jaskolski M]]
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[[Category: Michalska K]]
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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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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]
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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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[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Hernandez-Santoyo, A.]]
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[[Category: Jaskolski, M.]]
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[[Category: Michalska, K.]]
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[[Category: Asparaginase]]
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[[Category: Autoproteolysis]]
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[[Category: Isoaspartyl peptidase]]
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[[Category: Ntn-hydrolase]]
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[[Category: Precursor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:03:09 2008''
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Current revision

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

PDB ID 2zak

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