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| | <StructureSection load='1o7j' size='340' side='right'caption='[[1o7j]], [[Resolution|resolution]] 1.00Å' scene=''> | | <StructureSection load='1o7j' size='340' side='right'caption='[[1o7j]], [[Resolution|resolution]] 1.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1o7j]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O7J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1o7j]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Dickeya_chrysanthemi Dickeya chrysanthemi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O7J FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hfj|1hfj]], [[1hfk|1hfk]], [[1hfw|1hfw]], [[1hg0|1hg0]], [[1hg1|1hg1]], [[1jsl|1jsl]], [[1jsr|1jsr]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] </span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1o7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7j OCA], [https://pdbe.org/1o7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o7j RCSB], [https://www.ebi.ac.uk/pdbsum/1o7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7j ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7j OCA], [http://pdbe.org/1o7j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o7j RCSB], [http://www.ebi.ac.uk/pdbsum/1o7j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7j ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ASPG_DICCH ASPG_DICCH] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Asparaginase]] | + | [[Category: Dickeya chrysanthemi]] |
| - | [[Category: Erwinia chrysanthemi]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aghaiypour, K]] | + | [[Category: Aghaiypour K]] |
| - | [[Category: Dauter, M]] | + | [[Category: Dauter M]] |
| - | [[Category: Dauter, Z]] | + | [[Category: Dauter Z]] |
| - | [[Category: Lubkowski, J]] | + | [[Category: Lubkowski J]] |
| - | [[Category: Wlodawer, A]] | + | [[Category: Wlodawer A]] |
| - | [[Category: Atomic resolution]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: L-asparaginase]]
| + | |
| Structural highlights
Function
ASPG_DICCH
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
An X-ray structure of L-asparaginase from Erwinia chrysanthemi (ErA) has been refined at 1 A resolution to an R factor of below 0.1, using data collected on a synchrotron source. With four molecules of the enzyme consisting of 327 amino acids each, this crystal contains one of the largest asymmetric units of a protein refined to date at atomic resolution. Previously, structures of ErA and of related enzymes from other bacterial sources have been refined at resolutions not exceeding 1.7 A; thus, the present structure represents a very significant improvement in the quality of the available models of these proteins and should provide a good basis for future studies of the conformational variability of proteins, identification of subtle conformational features and corroboration of the stereochemical libraries, amongst other things. L-Asparaginases, which are enzymes that catalyze the hydrolysis of L-asparagine to aspartic acid, have been used for over 30 y as therapeutic agents in the treatment of acute childhood lymphoblastic leukemia, although the details of the enzymatic reaction and substrate specificity have not yet been completely elucidated. This atomic resolution structure is a step in that direction.
Atomic resolution structure of Erwinia chrysanthemi L-asparaginase.,Lubkowski J, Dauter M, Aghaiypour K, Wlodawer A, Dauter Z Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):84-92. Epub 2002, Dec 19. PMID:12499544[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lubkowski J, Dauter M, Aghaiypour K, Wlodawer A, Dauter Z. Atomic resolution structure of Erwinia chrysanthemi L-asparaginase. Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):84-92. Epub 2002, Dec 19. PMID:12499544
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