3c17

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{{Seed}}
 
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[[Image:3c17.png|left|200px]]
 
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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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The line below this paragraph, containing "STRUCTURE_3c17", creates the "Structure Box" on the page.
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<StructureSection load='3c17' size='340' side='right'caption='[[3c17]], [[Resolution|resolution]] 1.95&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'>[[3c17]] 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=3C17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C17 FirstGlance]. <br>
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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]] 1.95&#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></td></tr>
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{{STRUCTURE_3c17| PDB=3c17 | 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=3c17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c17 OCA], [https://pdbe.org/3c17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c17 RCSB], [https://www.ebi.ac.uk/pdbsum/3c17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c17 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/c1/3c17_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=3c17 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 l-asparaginases and their bacterial homologs, such as EcAIII found in Escherichia coli, form a subgroup of the N-terminal nucleophile (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 Thr(179) side chain rotation, identification of a potential general base residue, and the architecture of the oxyanion hole.
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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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The mechanism of autocatalytic activation of plant-type L-asparaginases.,Michalska K, Hernandez-Santoyo A, Jaskolski M J Biol Chem. 2008 May 9;283(19):13388-97. Epub 2008 Mar 10. PMID:18334484<ref>PMID:18334484</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 3c17" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18334484}}, 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 18334484 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_18334484}}
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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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3C17 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=3C17 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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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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[[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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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]
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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 Sun Jul 27 13:50:06 2008''
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Current revision

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

PDB ID 3c17

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