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1ult
From Proteopedia
(New page: 200px<br /><applet load="1ult" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ult, resolution 2.55Å" /> '''Crystal structure of...) |
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| - | [[Image:1ult.gif|left|200px]]<br /><applet load="1ult" size=" | + | [[Image:1ult.gif|left|200px]]<br /><applet load="1ult" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ult, resolution 2.55Å" /> | caption="1ult, resolution 2.55Å" /> | ||
'''Crystal structure of tt0168 from Thermus thermophilus HB8'''<br /> | '''Crystal structure of tt0168 from Thermus thermophilus HB8'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Long chain fatty acyl-CoA synthetases are responsible for fatty acid | + | 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== | ==About this Structure== | ||
| - | 1ULT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with CIT as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Long-chain-fatty-acid--CoA_ligase Long-chain-fatty-acid--CoA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.3 6.2.1.3] Full crystallographic information is available from [http:// | + | 1ULT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=CIT:'>CIT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Long-chain-fatty-acid--CoA_ligase Long-chain-fatty-acid--CoA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.3 6.2.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Miyano, M.]] | [[Category: Miyano, M.]] | ||
[[Category: Nakatsu, T.]] | [[Category: Nakatsu, T.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Sugahara, M.]] | [[Category: Sugahara, M.]] | ||
[[Category: Yamamoto, M.]] | [[Category: Yamamoto, M.]] | ||
| Line 34: | Line 34: | ||
[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:25:59 2008'' |
Revision as of 13:26, 21 February 2008
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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
1ULT is a Single protein structure of sequence from Thermus thermophilus with as ligand. Active as Long-chain-fatty-acid--CoA ligase, with EC number 6.2.1.3 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 Thu Feb 21 15:25:59 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. | CIT | Ligase | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics
