000			02219nam a2200265Ia 4500
003			MX-MdCICY
005			20250625140637.0
040			_cCICY
090			_aB-10772
245	1	0	_aElucidation of the Phosphate Binding Mode of DING Proteins Revealed by Subangstrom X-ray Crystallography
490	0		_vJ. Am. Chem. Soc., 22(131), p.7879-7886, 2009
520	3		_aPfluDING is a bacterial protein isolated from Pseudomonas fluorescens that belongs to the DING protein family, which is ubiquitous in eukaryotes and extends to prokaryotes. DING proteins and PfluDING have very similar topologies to phosphate Solute Binding Proteins (SBPs). The three-dimensional structure of PfluDING was obtained at subangstrom resolution (0.88 and 0.98 Å)at two different pH's (4.5 and 8.5), allowing us to discuss the hydrogen bond network that sequesters the phosphate ion in the binding site. From this high resolution data, we experimentally elucidated the molecular basis of phosphate binding in phosphate SBPs. The phosphate ion is tightly bound to the protein via 12 hydrogen bonds between phosphate oxygen atoms and OH and NH groups of the protein. The proton on one oxygen atom of the phosphate dianion forms a 2.5 Å low barrier hydrogen bond with an aspartate, with the energy released by forming this strong bond ensuring the specificity for the dianion even at pH 4.5. In particular, contrary to previous theories on phosphate SBPs, accurate electrostatic potential calculations show that the binding cleft is positively charged. PfluDING structures reveal that only dibasic phosphate binds to the protein at both acidic and basic phosphate, suggesting that the protein binding site environment stabilizes the HPO4 2- form of phosphate.
700	1	2	_aLiebschner, D.
700	1	2	_aElias, M.
700	1	2	_aMoniot, S.
700	1	2	_aFournier, B.
700	1	2	_aScott, K.
700	1	2	_aJelsch, C.
700	1	2	_aGuillot, B.
700	1	2	_aGuillot, B.
700	1	2	_aChabriere, E.
856	4	0	_uhttps://drive.google.com/file/d/1vNc8z15zYNCtAm9kfke9ZCX1elvNawpC/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
942			_2Loc _cREF1
008			250602s9999 xx |||||s2 |||| ||und|d
999			_c45004 _d45004