1ult
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Crystal structure of tt0168 from Thermus thermophilus HB8
OverviewOverview
Long chain fatty acyl-CoA synthetases are responsible for fatty acid, degradation as well as physiological regulation of cellular functions via, the production of long chain fatty acyl-CoA esters. We report the first, crystal structures of long chain fatty acyl-CoA synthetase homodimer, (LC-FACS) from Thermus thermophilus HB8 (ttLC-FACS), including complexes, with the ATP analogue adenosine 5'-(beta,gamma-imido) triphosphate, (AMP-PNP) and myristoyl-AMP. ttLC-FACS is a member of the adenylate, forming enzyme superfamily that catalyzes the ATP-dependent acylation of, fatty acid in a two-step reaction. The first reaction step was shown to, propagate in AMP-PNP complex crystals soaked with myristate solution., Myristoyl-AMP was identified as the intermediate. The AMP-PNP and the, myristoyl-AMP complex structures show an identical closed conformation of, the small C-terminal domains, whereas the uncomplexed form shows a variety, of open conformations. Upon ATP binding, the fatty acid-binding tunnel, gated by an aromatic residue opens to the ATP-binding site. The gated, fatty acid-binding tunnel appears only to allow one-way movement of the, fatty acid during overall catalysis. The protein incorporates a, hydrophobic branch from the fatty acid-binding tunnel that is responsible, for substrate specificity. Based on these high resolution crystal, structures, we propose a unidirectional Bi Uni Uni Bi Ping-Pong mechanism, for the two-step acylation by ttLC-FACS.
About this StructureAbout this Structure
1ULT is a Single protein structure of sequence from Thermus thermophilus with CIT as ligand. Active as Long-chain-fatty-acid--CoA ligase, with EC number 6.2.1.3 Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of the substrate-specific two-step catalysis of long chain fatty acyl-CoA synthetase dimer., Hisanaga Y, Ago H, Nakagawa N, Hamada K, Ida K, Yamamoto M, Hori T, Arii Y, Sugahara M, Kuramitsu S, Yokoyama S, Miyano M, J Biol Chem. 2004 Jul 23;279(30):31717-26. Epub 2004 May 15. PMID:15145952
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- Long-chain-fatty-acid--CoA ligase
- Single protein
- Thermus thermophilus
- Ago, H.
- Arii, Y.
- Hamada, K.
- Hisanaga, Y.
- Hori, T.
- Ida, K.
- Kanda, H.
- Kuramitsu, S.
- Miyano, M.
- Nakatsu, T.
- RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.
- Sugahara, M.
- Yamamoto, M.
- Yokoyama, S.
- CIT
- Ligase
- Riken structural genomics/proteomics initiative
- Rsgi
- Structural genomics