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2c8m

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[[Image:2c8m.png|left|200px]]
 
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{{STRUCTURE_2c8m| PDB=2c8m | SCENE= }}
{{STRUCTURE_2c8m| PDB=2c8m | SCENE= }}
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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===
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{{ABSTRACT_PUBMED_16384580}}
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==Function==
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[[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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{{ABSTRACT_PUBMED_16384580}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:016384580</ref><references group="xtra"/>
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<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

Template:STRUCTURE 2c8m

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
  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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

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