1hg0

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[[Image:1hg0.gif|left|200px]]
 
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==X-ray structure of the complex between Erwinia chrysanthemi L-asparaginase and succinic acid==
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The line below this paragraph, containing "STRUCTURE_1hg0", creates the "Structure Box" on the page.
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<StructureSection load='1hg0' size='340' side='right'caption='[[1hg0]], [[Resolution|resolution]] 1.90&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'>[[1hg0]] 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=1HG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HG0 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]] 1.9&#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=SIN:SUCCINIC+ACID'>SIN</scene></td></tr>
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{{STRUCTURE_1hg0| PDB=1hg0 | 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=1hg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hg0 OCA], [https://pdbe.org/1hg0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hg0 RCSB], [https://www.ebi.ac.uk/pdbsum/1hg0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hg0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ASPG_DICCH ASPG_DICCH]
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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/hg/1hg0_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=1hg0 ConSurf].
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<div style="clear:both"></div>
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'''X-RAY STRUCTURE OF THE COMPLEX BETWEEN ERWINIA CHRYSANTHEMI L-ASPARAGINASE AND SUCCINIC ACID'''
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==See Also==
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*[[Asparaginase 3D structures|Asparaginase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Bacterial L-asparaginases, enzymes that catalyze the hydrolysis of L-asparagine to aspartic acid, have been used for over 30 years as therapeutic agents in the treatment of acute childhood lymphoblastic leukemia. Other substrates of asparaginases include L-glutamine, D-asparagine, and succinic acid monoamide. In this report, we present high-resolution crystal structures of the complexes of Erwinia chrysanthemi L-asparaginase (ErA) with the products of such reactions that also can serve as substrates, namely L-glutamic acid (L-Glu), D-aspartic acid (D-Asp), and succinic acid (Suc). Comparison of the four independent active sites within each complex indicates unique and specific binding of the ligand molecules; the mode of binding is also similar between complexes. The lack of the alpha-NH3(+) group in Suc, compared to L-Asp, does not affect the binding mode. The side chain of L-Glu, larger than that of L-Asp, causes several structural distortions in the ErA active side. The active site flexible loop (residues 15-33) does not exhibit stable conformation, resulting in suboptimal orientation of the nucleophile, Thr15. Additionally, the delta-COO(-) plane of L-Glu is approximately perpendicular to the plane of gamma-COO(-) in L-Asp bound to the asparaginase active site. Binding of D-Asp to the ErA active site is very distinctive compared to the other ligands, suggesting that the low activity of ErA against D-Asp could be mainly attributed to the low k(cat) value. A comparison of the amino acid sequence and the crystal structure of ErA with those of other bacterial L-asparaginases shows that the presence of two active-site residues, Glu63(ErA) and Ser254(ErA), may correlate with significant glutaminase activity, while their substitution by Gln and Asn, respectively, may lead to minimal L-glutaminase activity.
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[[Category: Dickeya chrysanthemi]]
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[[Category: Large Structures]]
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==About this Structure==
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[[Category: Kolyani KA]]
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1HG0 is a [[Single protein]] structure of 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=1HG0 OCA].
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[[Category: Lubkowski J]]
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[[Category: Wlodawer A]]
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==Reference==
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Structural basis for the activity and substrate specificity of Erwinia chrysanthemi L-asparaginase., Aghaiypour K, Wlodawer A, Lubkowski J, Biochemistry. 2001 May 15;40(19):5655-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11341830 11341830]
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[[Category: Asparaginase]]
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[[Category: Erwinia chrysanthemi]]
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[[Category: Single protein]]
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[[Category: Kolyani, K A.]]
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[[Category: Lubkowski, J.]]
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[[Category: Wlodawer, A.]]
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[[Category: Asparaginase]]
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[[Category: Complex]]
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[[Category: D-aspartate]]
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[[Category: Hydrolase]]
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[[Category: Structure]]
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[[Category: X-ray]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:48:42 2008''
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Current revision

X-ray structure of the complex between Erwinia chrysanthemi L-asparaginase and succinic acid

PDB ID 1hg0

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