2zal
From Proteopedia
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[[Image:2zal.png|left|200px]] | [[Image:2zal.png|left|200px]] | ||
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==About this Structure== | ==About this Structure== | ||
- | + | [[2zal]] is a 4 chain structure of [[Aminopeptidase]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k12 Escherichia coli k12]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1seo 1seo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZAL OCA]. | |
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+ | ==See Also== | ||
+ | *[[Aminopeptidase]] | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:15946951</ref><ref group="xtra">PMID:11053866</ref><ref group="xtra">PMID:7477383</ref><ref group="xtra">PMID:9541410</ref><ref group="xtra">PMID:8846222</ref><ref group="xtra">PMID:9685368</ref><ref group="xtra">PMID:10490104</ref><ref group="xtra">PMID:14616088</ref><ref group="xtra">PMID:15159592</ref><references group="xtra"/> | <ref group="xtra">PMID:15946951</ref><ref group="xtra">PMID:11053866</ref><ref group="xtra">PMID:7477383</ref><ref group="xtra">PMID:9541410</ref><ref group="xtra">PMID:8846222</ref><ref group="xtra">PMID:9685368</ref><ref group="xtra">PMID:10490104</ref><ref group="xtra">PMID:14616088</ref><ref group="xtra">PMID:15159592</ref><references group="xtra"/> | ||
- | [[Category: Escherichia coli]] | + | [[Category: Escherichia coli k12]] |
[[Category: Brzezinski, K.]] | [[Category: Brzezinski, K.]] | ||
[[Category: Jaskolski, M.]] | [[Category: Jaskolski, M.]] | ||
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[[Category: L-aspartate/calcium cluster]] | [[Category: L-aspartate/calcium cluster]] | ||
[[Category: Ntn-hydrolase]] | [[Category: Ntn-hydrolase]] | ||
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 19:50:53 2009'' |
Revision as of 22:39, 14 March 2011
Contents |
Crystal structure of E. coli isoaspartyl aminopeptidase/L-asparaginase in complex with L-aspartate
Template:ABSTRACT PUBMED 15946951
About this Structure
2zal is a 4 chain structure of Aminopeptidase with sequence from Escherichia coli k12. This structure supersedes the now removed PDB entry 1seo. Full crystallographic information is available from OCA.
See Also
Reference
- 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
- 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
- Xuan J, Tarentino AL, Grimwood BG, Plummer TH Jr, Cui T, Guan C, Van Roey P. Crystal structure of glycosylasparaginase from Flavobacterium meningosepticum. Protein Sci. 1998 Mar;7(3):774-81. PMID:9541410
- Oinonen C, Tikkanen R, Rouvinen J, Peltonen L. Three-dimensional structure of human lysosomal aspartylglucosaminidase. Nat Struct Biol. 1995 Dec;2(12):1102-8. PMID:8846222
- Guo HC, Xu Q, Buckley D, Guan C. Crystal structures of Flavobacterium glycosylasparaginase. An N-terminal nucleophile hydrolase activated by intramolecular proteolysis. J Biol Chem. 1998 Aug 7;273(32):20205-12. PMID:9685368
- 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
- Saarela J, Oinonen C, Jalanko A, Rouvinen J, Peltonen L. Autoproteolytic activation of human aspartylglucosaminidase. Biochem J. 2004 Mar 1;378(Pt 2):363-71. PMID:14616088 doi:10.1042/BJ20031496
- 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