2c8m
From Proteopedia
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===STRUCTURE OF PROTEIN TA0514, PUTATIVE LIPOATE PROTEIN LIGASE FROM T. ACIDOPHILUM WITH BOUND LIPOIC ACID=== | ===STRUCTURE OF PROTEIN TA0514, PUTATIVE LIPOATE PROTEIN LIGASE FROM T. ACIDOPHILUM WITH BOUND LIPOIC ACID=== | ||
| + | {{ABSTRACT_PUBMED_16384580}} | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/LPLA_THEAC LPLA_THEAC]] Part of a lipoate-protein ligase complex that catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Can also use octanoate as substrate.<ref>PMID:16384580</ref> <ref>PMID:19594830</ref> <ref>PMID:19520844</ref> <ref>PMID:16141198</ref> | |
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:016384580</ref><references group="xtra"/> | + | <ref group="xtra">PMID:016384580</ref><references group="xtra"/><references/> |
[[Category: Thermoplasma acidophilum]] | [[Category: Thermoplasma acidophilum]] | ||
[[Category: Luisi, B F.]] | [[Category: Luisi, B F.]] | ||
Revision as of 08:35, 23 April 2014
Contents |
STRUCTURE OF PROTEIN TA0514, PUTATIVE LIPOATE PROTEIN LIGASE FROM T. ACIDOPHILUM WITH BOUND LIPOIC ACID
Template:ABSTRACT PUBMED 16384580
Function
[LPLA_THEAC] Part of a lipoate-protein ligase complex that catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Can also use octanoate as substrate.[1] [2] [3] [4]
About this Structure
2c8m is a 4 chain structure with sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA.
Reference
- McManus E, Luisi BF, Perham RN. Structure of a putative lipoate protein ligase from Thermoplasma acidophilum and the mechanism of target selection for post-translational modification. J Mol Biol. 2006 Feb 24;356(3):625-37. Epub 2005 Dec 5. PMID:16384580 doi:10.1016/j.jmb.2005.11.057
- ↑ McManus E, Luisi BF, Perham RN. Structure of a putative lipoate protein ligase from Thermoplasma acidophilum and the mechanism of target selection for post-translational modification. J Mol Biol. 2006 Feb 24;356(3):625-37. Epub 2005 Dec 5. PMID:16384580 doi:10.1016/j.jmb.2005.11.057
- ↑ Posner MG, Upadhyay A, Bagby S, Hough DW, Danson MJ. A unique lipoylation system in the Archaea. Lipoylation in Thermoplasma acidophilum requires two proteins. FEBS J. 2009 Aug;276(15):4012-22. doi: 10.1111/j.1742-4658.2009.07110.x. Epub, 2009 Jul 7. PMID:19594830 doi:http://dx.doi.org/10.1111/j.1742-4658.2009.07110.x
- ↑ Christensen QH, Cronan JE. The Thermoplasma acidophilum LplA-LplB complex defines a new class of bipartite lipoate-protein ligases. J Biol Chem. 2009 Aug 7;284(32):21317-26. doi: 10.1074/jbc.M109.015016. Epub 2009, Jun 11. PMID:19520844 doi:http://dx.doi.org/10.1074/jbc.M109.015016
- ↑ Kim DJ, Kim KH, Lee HH, Lee SJ, Ha JY, Yoon HJ, Suh SW. Crystal structure of lipoate-protein ligase A bound with the activated intermediate: insights into interaction with lipoyl domains. J Biol Chem. 2005 Nov 11;280(45):38081-9. Epub 2005 Sep 2. PMID:16141198 doi:10.1074/jbc.M507284200
