3pbk | pdb_00003pbk

Structural and Functional Studies of Fatty Acyl-Adenylate Ligases from E. coli and L. pneumophila

spinqualitylabelsall models 3pbk, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3pbk is a 2 chain structure with sequence from Escherichia coli O6. This structure supersedes the now removed PDB entry 3gqw. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Ligands: 1ZZ, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H2VDD9_ECOL6 Publication Abstract from PubMed 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 A, 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. Structural and Functional Studies of Fatty Acyl Adenylate Ligases from E. coli and L. pneumophila.,Zhang Z, Zhou R, Sauder JM, Tonge PJ, Burley SK, Swaminathan S J Mol Biol. 2010 Dec 23. PMID:21185305 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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