4eca: Difference between revisions
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|PDB= 4eca |SIZE=350|CAPTION= <scene name='initialview01'>4eca</scene>, resolution 2.2Å | |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> | |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= | |LIGAND= <scene name='pdbligand=AEI:THREONINE-ASPARTIC+ESTER'>AEI</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] | |ACTIVITY= <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> | ||
|GENE= ANSB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= ANSB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4eca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eca OCA], [http://www.ebi.ac.uk/pdbsum/4eca PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=4eca RCSB]</span> | |||
}} | }} | ||
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[[Category: threonine amidohydrolase]] | [[Category: threonine amidohydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:38:33 2008'' | ||
Revision as of 05:38, 31 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | |||||||
| Gene: | ANSB (Escherichia coli) | ||||||
| Activity: | Asparaginase, with EC number 3.5.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ASPARAGINASE FROM E. COLI, MUTANT T89V WITH COVALENTLY BOUND ASPARTATE
OverviewOverview
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 StructureAbout this Structure
4ECA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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
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