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1ult

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{{Structure
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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{{STRUCTURE_1ult| PDB=1ult | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ult FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ult OCA], [http://www.ebi.ac.uk/pdbsum/1ult PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ult RCSB]</span>
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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.]]
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[[Category: Ligase]]
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Revision as of 08:24, 3 May 2008

Image:1ult.gif

Template:STRUCTURE 1ult

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. 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 11:24:09 2008

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