1t3m
From Proteopedia
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|PDB= 1t3m |SIZE=350|CAPTION= <scene name='initialview01'>1t3m</scene>, resolution 1.65Å | |PDB= 1t3m |SIZE=350|CAPTION= <scene name='initialview01'>1t3m</scene>, resolution 1.65Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> | + | |LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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= YBIK, B0828 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= YBIK, B0828 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1jn9|1jn9]], [[1k2x|1k2x]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t3m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t3m OCA], [http://www.ebi.ac.uk/pdbsum/1t3m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t3m RCSB]</span> | ||
}} | }} | ||
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[[Category: Pazgier, M.]] | [[Category: Pazgier, M.]] | ||
[[Category: Prahl, A.]] | [[Category: Prahl, A.]] | ||
| - | [[Category: NA]] | ||
| - | [[Category: NO3]] | ||
[[Category: isoaspartyl peptidase]] | [[Category: isoaspartyl peptidase]] | ||
[[Category: plant-type asparaginase]] | [[Category: plant-type asparaginase]] | ||
[[Category: type iii l-asparaginase]] | [[Category: type iii l-asparaginase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:50:50 2008'' |
Revision as of 20:50, 30 March 2008
| |||||||
| , resolution 1.65Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | YBIK, B0828 (Escherichia coli) | ||||||
| Activity: | Asparaginase, with EC number 3.5.1.1 | ||||||
| Related: | 1jn9, 1k2x
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the isoaspartyl peptidase with L-asparaginase activity from E. coli
Overview
The crystal structure of the Escherichia coli enzyme (EcAIII) with isoaspartyl dipeptidase and L-asparaginase activity has been solved and refined to a resolution of 1.65 angstroms, with crystallographic R-factor and Rfree values of 0.178 and 0.209, respectively. EcAIII belongs to the family of N-terminal hydrolases. The amino-acid sequence of EcAIII is homologous to those of putative asparaginases from plants. The structure of EcAIII is similar to the structures of glycosylasparaginases. The mature and catalytically active form of EcAIII is a heterotetramer consisting of two alpha-subunits and two beta-subunits. Both of the equivalent active sites present in the EcAIII tetramer is assisted by a metal-binding site. The metal cations, modelled here as Na+, have not previously been observed in glycosylasparaginases. This reported structure helps to explain the inability of EcAIII and other plant-type asparaginases to hydrolyze N4-(beta-N-acetylglucosaminyl)-L-asparagine, the substrate of glycosylasparaginases.
About this Structure
1T3M is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of the isoaspartyl peptidase with L-asparaginase activity from Escherichia coli., Prahl A, Pazgier M, Hejazi M, Lockau W, Lubkowski J, Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1173-6. Epub 2004, May 21. PMID:15159592
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