3c17
From Proteopedia
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[[Image:3c17.png|left|200px]] | [[Image:3c17.png|left|200px]] | ||
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==About this Structure== | ==About this Structure== | ||
- | + | [[3c17]] is a 2 chain structure of [[Aminopeptidase]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k12 Escherichia coli k12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C17 OCA]. | |
+ | |||
+ | ==See Also== | ||
+ | *[[Aminopeptidase]] | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:18334484</ref><ref group="xtra">PMID:15946951</ref><ref group="xtra">PMID:11053866</ref><ref group="xtra">PMID:16725155</ref><ref group="xtra">PMID:15159592</ref><ref group="xtra">PMID:10490104</ref><ref group="xtra">PMID:9545304</ref><ref group="xtra">PMID:9737998</ref><ref group="xtra">PMID:12906830</ref><ref group="xtra">PMID:7477383</ref><references group="xtra"/> | <ref group="xtra">PMID:18334484</ref><ref group="xtra">PMID:15946951</ref><ref group="xtra">PMID:11053866</ref><ref group="xtra">PMID:16725155</ref><ref group="xtra">PMID:15159592</ref><ref group="xtra">PMID:10490104</ref><ref group="xtra">PMID:9545304</ref><ref group="xtra">PMID:9737998</ref><ref group="xtra">PMID:12906830</ref><ref group="xtra">PMID:7477383</ref><references group="xtra"/> | ||
- | [[Category: Escherichia coli]] | + | [[Category: Escherichia coli k12]] |
[[Category: Hernandez-Santoyo, A.]] | [[Category: Hernandez-Santoyo, A.]] | ||
[[Category: Jaskolski, M.]] | [[Category: Jaskolski, M.]] | ||
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[[Category: Ntn-hydrolase]] | [[Category: Ntn-hydrolase]] | ||
[[Category: Precursor]] | [[Category: Precursor]] | ||
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 11:44:59 2009'' |
Revision as of 21:10, 14 March 2011
Contents |
Hexagonal Crystal Structure of Precursor E. coli Isoaspartyl Peptidase/l-Asparaginase (ECAIII) with Active-site T179A mutation
Template:ABSTRACT PUBMED 18334484
About this Structure
3c17 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, Hernandez-Santoyo A, Jaskolski M. The mechanism of autocatalytic activation of plant-type L-asparaginases. J Biol Chem. 2008 May 9;283(19):13388-97. Epub 2008 Mar 10. PMID:18334484 doi:10.1074/jbc.M800746200
- 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
- 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
- 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