4eca
From Proteopedia
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| - | [[Image:4eca.jpg|left|200px]] | + | [[Image:4eca.jpg|left|200px]] |
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| - | '''ASPARAGINASE FROM E. COLI, MUTANT T89V WITH COVALENTLY BOUND ASPARTATE''' | + | {{Structure |
| + | |PDB= 4eca |SIZE=350|CAPTION= <scene name='initialview01'>4eca</scene>, resolution 2.2Å | ||
| + | |SITE= <scene name='pdbsite=AS:Active+Site+In+Monomer+A'>AS</scene>, <scene name='pdbsite=BS:Active+Site+In+Monomer+B'>BS</scene>, <scene name='pdbsite=CS:Active+Site+In+Monomer+C'>CS</scene> and <scene name='pdbsite=DS:Active+Site+In+Monomer+D'>DS</scene> | ||
| + | |LIGAND= | ||
| + | |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= ANSB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''ASPARAGINASE FROM E. COLI, MUTANT T89V WITH COVALENTLY BOUND ASPARTATE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 4ECA is a [ | + | 4ECA 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=4ECA OCA]. |
==Reference== | ==Reference== | ||
| - | A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant., Palm GJ, Lubkowski J, Derst C, Schleper S, Rohm KH, Wlodawer A, FEBS Lett. 1996 Jul 22;390(2):211-6. PMID:[http:// | + | A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant., Palm GJ, Lubkowski J, Derst C, Schleper S, Rohm KH, Wlodawer A, FEBS Lett. 1996 Jul 22;390(2):211-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8706862 8706862] |
[[Category: Asparaginase]] | [[Category: Asparaginase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: threonine amidohydrolase]] | [[Category: threonine amidohydrolase]] | ||
| - | ''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 19:09:31 2008'' |
Revision as of 17:09, 20 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Gene: | ANSB (Escherichia coli) | ||||||
| Activity: | Asparaginase, with EC number 3.5.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ASPARAGINASE FROM E. COLI, MUTANT T89V WITH COVALENTLY BOUND ASPARTATE
Overview
Escherichia coli asparaginase II catalyzes the hydrolysis of L-asparagine to L-aspartate via a threonine-bound acyl-enzyme intermediate. A nearly inactive mutant in which one of the active site threonines, Thr-89, was replaced by valine was constructed, expressed, and crystallized. Its structure, solved at 2.2 A resolution, shows high overall similarity to the wild-type enzyme, but an aspartyl moiety is covalently bound to Thr-12, resembling a reaction intermediate. Kinetic analysis confirms the deacylation deficiency, which is also explained on a structural basis. The previously identified oxyanion hole is described in more detail.
About this Structure
4ECA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant., Palm GJ, Lubkowski J, Derst C, Schleper S, Rohm KH, Wlodawer A, FEBS Lett. 1996 Jul 22;390(2):211-6. PMID:8706862
Page seeded by OCA on Thu Mar 20 19:09:31 2008
