3dgn

A non-biological ATP binding protein crystallized in the presence of 100 mM ADP

spinqualitylabelsall models 3dgn, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3dgn is a 1 chain structure with sequence from Miscellaneous nucleic acid. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, PEG, ZN Related: 2p05, 2p09, 3dgl, 3dgm, 3dgo Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed How primitive enzymes emerged from a primordial pool remains a fundamental unanswered question with important practical implications in synthetic biology. Here we show that a de novo evolved ATP binding protein, selected solely on the basis of its ability to bind ATP, mediates the regiospecific hydrolysis of ATP to ADP when crystallized with 1 equiv of ATP. Structural insights into this reaction were obtained by growing protein crystals under saturating ATP conditions. The resulting crystal structure refined to 1.8 A resolution reveals that this man-made protein binds ATP in an unusual bent conformation that is metal-independent and held in place by a key bridging water molecule. Removal of this interaction using a null mutant results in a variant that binds ATP in a normal linear geometry and is incapable of ATP hydrolysis. Biochemical analysis, including high-resolution mass spectrometry performed on dissolved protein crystals, confirms that the reaction is accelerated in the crystalline environment. This observation suggests that proteins with weak chemical reactivity can emerge from high affinity ligand binding sites and that constrained ligand-binding geometries could have helped to facilitate the emergence of early protein enzymes. A synthetic protein selected for ligand binding affinity mediates ATP hydrolysis.,Simmons CR, Stomel JM, McConnell MD, Smith DA, Watkins JL, Allen JP, Chaput JC ACS Chem Biol. 2009 Aug 21;4(8):649-58. PMID:19522480 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA