1v26
From Proteopedia
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'''Crystal structure of tt0168 from Thermus thermophilus HB8''' | '''Crystal structure of tt0168 from Thermus thermophilus HB8''' | ||
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[[Category: Yamamoto, M.]] | [[Category: Yamamoto, M.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
| - | [[Category: | + | [[Category: Ligase]] |
| - | [[Category: | + | [[Category: Riken structural genomics/proteomics initiative]] |
| - | [[Category: | + | [[Category: Rsgi]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:59:02 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 08:59, 3 May 2008
Crystal structure of tt0168 from Thermus thermophilus HB8
Overview
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 Structure
1V26 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 11:59:02 2008
Categories: 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. | Ligase | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic
