2z1z
From Proteopedia
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{{STRUCTURE_2z1z| PDB=2z1z | SCENE= }} | {{STRUCTURE_2z1z| PDB=2z1z | SCENE= }} | ||
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===Crystal structure of LL-Diaminopimelate Aminotransferase from Arabidopsis thaliana complexed with L-malate ion=== | ===Crystal structure of LL-Diaminopimelate Aminotransferase from Arabidopsis thaliana complexed with L-malate ion=== | ||
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{{ABSTRACT_PUBMED_17583737}} | {{ABSTRACT_PUBMED_17583737}} | ||
==About this Structure== | ==About this Structure== | ||
[[2z1z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z1Z OCA]. | [[2z1z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z1Z OCA]. | ||
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| + | ==See Also== | ||
| + | *[[Journal:Acta Cryst F:2|Journal:Acta Cryst F:2]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:017583737</ref><references group="xtra"/> | + | <ref group="xtra">PMID:017583737</ref><ref group="xtra">PMID:000000000</ref><references group="xtra"/><references/> |
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: LL-diaminopimelate aminotransferase]] | [[Category: LL-diaminopimelate aminotransferase]] | ||
Revision as of 12:35, 7 April 2013
Contents |
Crystal structure of LL-Diaminopimelate Aminotransferase from Arabidopsis thaliana complexed with L-malate ion
Template:ABSTRACT PUBMED 17583737
About this Structure
2z1z is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.
See Also
Reference
- Watanabe N, Cherney MM, van Belkum MJ, Marcus SL, Flegel MD, Clay MD, Deyholos MK, Vederas JC, James MN. Crystal structure of LL-diaminopimelate aminotransferase from Arabidopsis thaliana: a recently discovered enzyme in the biosynthesis of L-lysine by plants and Chlamydia. J Mol Biol. 2007 Aug 17;371(3):685-702. Epub 2007 May 26. PMID:17583737 doi:10.1016/j.jmb.2007.05.061
- Steere AN, Byrne SL, Chasteen ND, Smith VC, Macgillivray RT, Mason AB. Evidence that His349 acts as a pH-inducible switch to accelerate receptor-mediated iron release from the C-lobe of human transferrin. J Biol Inorg Chem. 2010 Aug 14. PMID:20711621 doi:10.1007/s00775-010-0694-2 20711621 10.1007/s00775-010-0694-2
Categories: Arabidopsis thaliana | LL-diaminopimelate aminotransferase | Belkum, M J.van. | Cherney, M M. | Clay, M D. | Deyholos, M K. | Flegel, M D. | James, M N.G. | Marcus, S L. | Vederas, J C. | Watanabe, N. | Ll-dap | Ll-dap-at | Ll-diaminopimelate aminotransferase | Lysine biosynthesis | Plp | Thdpa | Transferase
