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1t3m

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{{STRUCTURE_1t3m| PDB=1t3m | SCENE= }}
{{STRUCTURE_1t3m| PDB=1t3m | SCENE= }}
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'''Structure of the isoaspartyl peptidase with L-asparaginase activity from E. coli'''
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===Structure of the isoaspartyl peptidase with L-asparaginase activity from E. coli===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15159592 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15159592}}
==About this Structure==
==About this Structure==
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[[Category: Plant-type asparaginase]]
[[Category: Plant-type asparaginase]]
[[Category: Type iii l-asparaginase]]
[[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 Jul 27 17:49:57 2008''

Revision as of 14:50, 27 July 2008

Image:1t3m.png

Template:STRUCTURE 1t3m

Structure of the isoaspartyl peptidase with L-asparaginase activity from E. coli

Template:ABSTRACT PUBMED 15159592

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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