3KXW

The crystal structure of fatty acid AMP ligase from Legionella pneumophila

3KXW の概要

• エントリーDOI: 10.2210/pdb3kxw/pdb
• 分子名称: Saframycin Mx1 synthetase B, 5'-O-[(S)-(dodecanoyloxy)(hydroxy)phosphoryl]adenosine (3 entities in total)
• 機能のキーワード: fatty acid amp ligase, sgx, acyl adenylate, structural genomics, psi-2, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, ligase
• 由来する生物種: Legionella pneumophila subsp. pneumophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 68394.05

構造登録者

Zhang, Z.,Burley, S.K.,Swaminathan, S.,New York SGX Research Center for Structural Genomics (NYSGXRC) (登録日: 2009-12-04, 公開日: 2010-03-16, 最終更新日: 2024-11-06)

主引用文献

Zhang, Z.,Zhou, R.,Sauder, J.M.,Tonge, P.J.,Burley, S.K.,Swaminathan, S.
Structural and Functional Studies of Fatty Acyl Adenylate Ligases from E. coli and L. pneumophila.
J.Mol.Biol., 406:313-324, 2011

PubMed Abstract: Fatty acyl-AMP ligase (FAAL) is a new member of a family of adenylate-forming enzymes that were recently discovered in Mycobacterium tuberculosis. They are similar in sequence to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, while FACLs perform a two-step catalytic reaction, AMP ligation followed by CoA ligation using ATP and CoA as cofactors, FAALs produce only the acyl adenylate and are unable to perform the second step. We report X-ray crystal structures of full-length FAAL from Escherichia coli (EcFAAL) and FAAL from Legionella pneumophila (LpFAAL) bound to acyl adenylate, determined at resolution limits of 3.0 and 1.85 Å, respectively. The structures share a larger N-terminal domain and a smaller C-terminal domain, which together resemble the previously determined structures of FAAL and FACL proteins. Our two structures occur in quite different conformations. EcFAAL adopts the adenylate-forming conformation typical of FACLs, whereas LpFAAL exhibits a unique intermediate conformation. Both EcFAAL and LpFAAL have insertion motifs that distinguish them from the FACLs. Structures of EcFAAL and LpFAAL reveal detailed interactions between this insertion motif and the interdomain hinge region and with the C-terminal domain. We suggest that the insertion motifs support sufficient interdomain motions to allow substrate binding and product release during acyl adenylate formation, but they preclude CoA binding, thereby preventing CoA ligation.

PubMed: 21185305
DOI: 10.1016/j.jmb.2010.12.011

実験手法

X-RAY DIFFRACTION (1.851 Å)