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1hfw
From Proteopedia
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| - | [[Image:1hfw.gif|left|200px]] | + | [[Image:1hfw.gif|left|200px]] |
| - | + | ||
| - | '''X-RAY STRUCTURE OF THE COMPLEX BETWEEN ERWINIA CHRYSANTHEMI L-ASPARAGINASE AND L-GLUTAMATE''' | + | {{Structure |
| + | |PDB= 1hfw |SIZE=350|CAPTION= <scene name='initialview01'>1hfw</scene>, resolution 1.80Å | ||
| + | |SITE= <scene name='pdbsite=AS1:Active+Site+Chain+A,+TYR-A29+Not+Visible+In+Electron+Density'>AS1</scene>, <scene name='pdbsite=AS2:Active+Site+Chain+B,+TYR-B29+Not+Visible+In+Electron+Density'>AS2</scene>, <scene name='pdbsite=AS3:Active+Site+Chain+C,+TYR-C29+Not+Visible+In+Electron+Density'>AS3</scene>, <scene name='pdbsite=AS4:Active+Site+Chain+D,+TYR-D29+Not+Visible+In+Electron+Density'>AS4</scene>, <scene name='pdbsite=LI1:GLU+Binding+Site+For+Chain+A'>LI1</scene>, <scene name='pdbsite=LI2:GLU+Binding+Site+For+Chain+B'>LI2</scene>, <scene name='pdbsite=LI3:GLU+Binding+Site+For+Chain+C'>LI3</scene> and <scene name='pdbsite=LI4:GLU+Binding+Site+For+Chain+D'>LI4</scene> | ||
| + | |LIGAND= <scene name='pdbligand=GLU:GLUTAMIC ACID'>GLU</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''X-RAY STRUCTURE OF THE COMPLEX BETWEEN ERWINIA CHRYSANTHEMI L-ASPARAGINASE AND L-GLUTAMATE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HFW is a [ | + | 1HFW 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=1HFW OCA]. |
==Reference== | ==Reference== | ||
| - | 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:// | + | 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] |
[[Category: Asparaginase]] | [[Category: Asparaginase]] | ||
[[Category: Erwinia chrysanthemi]] | [[Category: Erwinia chrysanthemi]] | ||
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[[Category: x-ray]] | [[Category: x-ray]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:36:35 2008'' |
Revision as of 09:36, 20 March 2008
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| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , and | ||||||
| Ligands: | |||||||
| Activity: | Asparaginase, with EC number 3.5.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-RAY STRUCTURE OF THE COMPLEX BETWEEN ERWINIA CHRYSANTHEMI L-ASPARAGINASE AND L-GLUTAMATE
Overview
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.
About this Structure
1HFW is a Single protein structure of sequence from Erwinia chrysanthemi. Full crystallographic information is available from OCA.
Reference
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:11341830
Page seeded by OCA on Thu Mar 20 11:36:35 2008
Categories: Asparaginase | Erwinia chrysanthemi | Single protein | Kolyani, K A. | Lubkowski, J. | Wlodawer, A. | GLU | Complex | D-aspartate | Hydrolase | Structure | X-ray
