1v25: Difference between revisions
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[[Image:1v25.gif|left|200px]] | [[Image:1v25.gif|left|200px]] | ||
'''Crystal structure of tt0168 from Thermus thermophilus HB8''' | {{Structure | ||
|PDB= 1v25 |SIZE=350|CAPTION= <scene name='initialview01'>1v25</scene>, resolution 2.30Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'>ANP</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''Crystal structure of tt0168 from Thermus thermophilus HB8''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1V25 is a [ | 1V25 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V25 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15145952 15145952] | ||
[[Category: Long-chain-fatty-acid--CoA ligase]] | [[Category: Long-chain-fatty-acid--CoA ligase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
[[Category: structural | [[Category: structural genomic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:39:46 2008'' | ||
Revision as of 15:39, 20 March 2008
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| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Long-chain-fatty-acid--CoA ligase, with EC number 6.2.1.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
1V25 is a Single protein structure of sequence from Thermus thermophilus. 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- 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.
- ANP
- MG
- Ligase
- Riken structural genomics/proteomics initiative
- Rsgi
- Structural genomic