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3en0
From Proteopedia
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{{STRUCTURE_3en0| PDB=3en0 | SCENE= }} | {{STRUCTURE_3en0| PDB=3en0 | SCENE= }} | ||
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===The Structure of Cyanophycinase=== | ===The Structure of Cyanophycinase=== | ||
| + | {{ABSTRACT_PUBMED_19591842}} | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/CPHB_SYNY3 CPHB_SYNY3]] Exopeptidase that catalyzes the hydrolytic cleavage of multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer) into aspartate-arginine dipeptides. | |
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| - | -- | + | |
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==About this Structure== | ==About this Structure== | ||
| - | [[3en0]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. | + | [[3en0]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EN0 OCA]. |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:019591842</ref><references group="xtra"/> | + | <ref group="xtra">PMID:019591842</ref><references group="xtra"/><references/> |
[[Category: Cyanophycinase]] | [[Category: Cyanophycinase]] | ||
| - | [[Category: Synechocystis sp. | + | [[Category: Synechocystis sp.]] |
[[Category: Kimber, M S.]] | [[Category: Kimber, M S.]] | ||
[[Category: Lai, S W.S.]] | [[Category: Lai, S W.S.]] | ||
Revision as of 09:29, 27 March 2013
Contents |
The Structure of Cyanophycinase
Template:ABSTRACT PUBMED 19591842
Function
[CPHB_SYNY3] Exopeptidase that catalyzes the hydrolytic cleavage of multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer) into aspartate-arginine dipeptides.
About this Structure
3en0 is a 3 chain structure with sequence from Synechocystis sp.. Full crystallographic information is available from OCA.
Reference
- Law AM, Lai SW, Tavares J, Kimber MS. The structural basis of beta-peptide-specific cleavage by the serine protease cyanophycinase. J Mol Biol. 2009 Sep 18;392(2):393-404. Epub 2009 Jul 8. PMID:19591842 doi:10.1016/j.jmb.2009.07.001
