1t3m

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[[Image:1t3m.jpg|left|200px]]
[[Image:1t3m.jpg|left|200px]]
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{{Structure
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|PDB= 1t3m |SIZE=350|CAPTION= <scene name='initialview01'>1t3m</scene>, resolution 1.65&Aring;
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The line below this paragraph, containing "STRUCTURE_1t3m", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE= YBIK, B0828 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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{{STRUCTURE_1t3m| PDB=1t3m | SCENE= }}
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|RELATEDENTRY=[[1jn9|1jn9]], [[1k2x|1k2x]]
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|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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'''Structure of the isoaspartyl peptidase with L-asparaginase activity from E. coli'''
'''Structure of the isoaspartyl peptidase with L-asparaginase activity from E. coli'''
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[[Category: Pazgier, M.]]
[[Category: Pazgier, M.]]
[[Category: Prahl, A.]]
[[Category: Prahl, A.]]
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[[Category: isoaspartyl peptidase]]
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[[Category: Isoaspartyl peptidase]]
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[[Category: plant-type asparaginase]]
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[[Category: Plant-type asparaginase]]
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[[Category: type iii l-asparaginase]]
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[[Category: Type iii l-asparaginase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:29:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:50:50 2008''
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Revision as of 06:29, 3 May 2008

Image:1t3m.jpg

Template:STRUCTURE 1t3m

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 Page seeded by OCA on Sat May 3 09:29:03 2008

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