This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2zak
From Proteopedia
(Difference between revisions)
m (Protected "2zak" [edit=sysop:move=sysop]) |
Revision as of 23:31, 14 March 2011
Contents |
Orthorhombic crystal structure of precursor E. coli isoaspartyl peptidase/L-asparaginase (EcAIII) with active-site T179A mutation
Template:ABSTRACT PUBMED 18323626
About this Structure
2zak is a 2 chain structure of Aminopeptidase with sequence from Escherichia coli k12. Full crystallographic information is available from OCA.
See Also
Reference
- Michalska K, Borek D, Hernandez-Santoyo A, Jaskolski M. Crystal packing of plant-type L-asparaginase from Escherichia coli. Acta Crystallogr D Biol Crystallogr. 2008 Mar;64(Pt 3):309-20. Epub 2008, Feb 20. PMID:18323626 doi:10.1107/S0907444907068072
- Michalska K, Brzezinski K, Jaskolski M. Crystal structure of isoaspartyl aminopeptidase in complex with L-aspartate. J Biol Chem. 2005 Aug 5;280(31):28484-91. Epub 2005 Jun 9. PMID:15946951 doi:10.1074/jbc.M504501200
- Borek D, Jaskolski M. Crystallization and preliminary crystallographic studies of a new L-asparaginase encoded by the Escherichia coli genome. Acta Crystallogr D Biol Crystallogr. 2000 Nov;56(Pt 11):1505-7. PMID:11053866
- Michalska K, Bujacz G, Jaskolski M. Crystal structure of plant asparaginase. J Mol Biol. 2006 Jun 30;360(1):105-16. Epub 2006 May 15. PMID:16725155 doi:10.1016/j.jmb.2006.04.066
- Brannigan JA, Dodson G, Duggleby HJ, Moody PC, Smith JL, Tomchick DR, Murzin AG. A protein catalytic framework with an N-terminal nucleophile is capable of self-activation. Nature. 1995 Nov 23;378(6555):416-9. PMID:7477383 doi:http://dx.doi.org/10.1038/378416a0
- Prahl A, Pazgier M, Hejazi M, Lockau W, Lubkowski J. Structure of the isoaspartyl peptidase with L-asparaginase activity from Escherichia coli. Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1173-6. Epub 2004, May 21. PMID:15159592 doi:10.1107/S0907444904003403
- Xu Q, Buckley D, Guan C, Guo HC. Structural insights into the mechanism of intramolecular proteolysis. Cell. 1999 Sep 3;98(5):651-61. PMID:10490104
- Guan C, Liu Y, Shao Y, Cui T, Liao W, Ewel A, Whitaker R, Paulus H. Characterization and functional analysis of the cis-autoproteolysis active center of glycosylasparaginase. J Biol Chem. 1998 Apr 17;273(16):9695-702. PMID:9545304
- Saarela J, Laine M, Tikkanen R, Oinonen C, Jalanko A, Rouvinen J, Peltonen L. Activation and oligomerization of aspartylglucosaminidase. J Biol Chem. 1998 Sep 25;273(39):25320-8. PMID:9737998
- Qian X, Guan C, Guo HC. A dual role for an aspartic acid in glycosylasparaginase autoproteolysis. Structure. 2003 Aug;11(8):997-1003. PMID:12906830
