Structure of protein Ta0514, putative lipoate protein ligase from T. acidophilum.Structure of protein Ta0514, putative lipoate protein ligase from T. acidophilum.

Structural highlights

2c7i is a 4 chain structure with sequence from Thermoplasma acidophilum DSM 1728. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LPLAN_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]

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. 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
  2. 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
  3. 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

2c7i, resolution 2.10Å

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