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1hfw

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[[Image:1hfw.gif|left|200px]]<br />
 
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<applet load="1hfw" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hfw, resolution 1.80&Aring;" />
 
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'''X-RAY STRUCTURE OF THE COMPLEX BETWEEN ERWINIA CHRYSANTHEMI L-ASPARAGINASE AND L-GLUTAMATE'''<br />
 
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==Overview==
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==X-ray structure of the complex between Erwinia chrysanthemi L-asparaginase and L-Glutamate==
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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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<StructureSection load='1hfw' size='340' side='right'caption='[[1hfw]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1hfw]] 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=1HFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HFW 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]] 1.8&#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=GLU:GLUTAMIC+ACID'>GLU</scene></td></tr>
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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=1hfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hfw OCA], [https://pdbe.org/1hfw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hfw RCSB], [https://www.ebi.ac.uk/pdbsum/1hfw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hfw 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/hf/1hfw_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=1hfw ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1HFW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi] with GLU as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Structure known Active Sites: AS1, AS2, AS3, AS4, LI1, LI2, LI3 and LI4. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HFW OCA].
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*[[Asparaginase 3D structures|Asparaginase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11341830 11341830]
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[[Category: Dickeya chrysanthemi]]
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[[Category: Asparaginase]]
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[[Category: Large Structures]]
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[[Category: Erwinia chrysanthemi]]
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[[Category: Kolyani KA]]
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[[Category: Single protein]]
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[[Category: Lubkowski J]]
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[[Category: Kolyani, K.A.]]
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[[Category: Wlodawer A]]
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[[Category: Lubkowski, J.]]
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[[Category: Wlodawer, A.]]
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[[Category: GLU]]
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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://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:00:14 2007''
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Current revision

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

PDB ID 1hfw

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