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Author(s): LOWRY DF; COOL RH; REDFIELD AG; PARMEGGIANI A
Title: NMR-STUDY OF THE PHOSPHATE-BINDING ELEMENTS OF ESCHERICHIA-COLI ELONGATION FACTOR-TU CATALYTIC DOMAIN
Source: BIOCHEMISTRY 30 (45): 10872-10877
Date: 1991 NOV 12
Document Type: Journal : Article
DOI:
Language: English
Comment:
Address: BRANDEIS UNIV,DEPT BIOCHEM,WALTHAM,MA 02254.
ECOLE POLYTECH,BIOCHIM LAB,CNRS,SDI 61480,F-91128 PALAISEAU,FRANCE. BRANDEIS UNIV,DEPT PHYS,WALTHAM,MA 02254. Reprint:
E-mail:
Abstract: The phosphoryl-binding elements in the GDP-binding domain of elongation factor Tu were studied by heteronuclear proton observe methods. Five proton resonances were found below 10.5 ppm. Two of these were assigned to the amide groups of Lys 24 and Gly 83. These are conserved residues in each of the consensus sequences. Their uncharacteristic downfield proton shifts are attributed to strong hydrogen bonds to phosphate oxygens as for resonances in N-ras-p2l [Redfield, A. G., & Papastavros, M. Z. (1990) Biochemistry 29, 3509-3514]. The Lys 24 of the EF-Tu G-domain has nearly the same proton and nitrogen shifts as the corresponding Lys 16 in p2l. These results suggest that this conserved lysine has a similar structural role in proteins in this class. The tentative Gly 83 resonance has no spectral analogue in p2l. A mutant protein with His 84 changed to glycine was fully N-15-labeled and the proton resonance assigned to Gly 83 shifted downfield by 0.3 ppm, thereby supporting the assignment.
Cited References: BACHOVCHIN WW, 1986, BIOCHEMISTRY-US, V25, P7751 BAX A, 1983, J MAGN RESON, V55, P301 BOURNE HR, 1990, NATURE, V348, P125 BOURNE HR, 1991, NATURE, V349, P117 CAMPBELLBURK S, 1988, P NATL ACAD SCI USA, V86, P817 CAMPBELLBURK S, 1989, BIOCHEMISTRY-US, V28, P9478 CLARK BFC, 1990, BIOCHIM BIOPHYS ACTA, V1050, P203 COOL RH, 1990, J BIOL CHEM, V265, P6744 COOL RH, 1991, BIOCHEMISTRY-US, V30, P362 DEVER TE, 1989, NATO ASI SER, P35 GRIFFEY RH, 1987, Q REV BIOPHYS, V19, P51 GUMUSEL F, 1990, BIOCHIM BIOPHYS ACTA, V1050, P215 HARMARK K, 1990, EUR J BIOCHEM, V194, P341 HATATANAKA A, 1989, BIOCHEMISTRY-US, V28, P9550 JACQUET E, 1988, EMBO J, V7, P2861 JACQUET E, 1989, EUR J BIOCHEM, V185, P341 JENSEN M, 1989, EUR J BIOCHEM, V182, P247 JURNAK F, 1985, SCIENCE, V230, P32 JURNAK F, 1990, BIOCHIM BIOPHYS ACTA, V1050, P204 KOSEN PA, 1989, METHOD ENZYMOL, V177, P86 LACOUR TFM, 1985, EMBO J, V4, P2385 MCCORMICK F, 1985, SCIENCE, V230, P78 MCINTOSH LP, 1987, P NATL ACAD SCI USA, V84, P1244 MILBURN MV, 1990, SCIENCE, V247, P939 MUCHMORE DC, 1989, METHOD ENZYMOL, V177, P44 NORSKOVLAURITSE.L, 1985, SCIENCE, V230, P78 PAI EF, 1989, NATURE, V341, P209 PAI EF, 1990, EMBO J, V9, P2351 PARMEGGIANI A, 1987, P NATL ACAD SCI USA, V84, P3141 REDFIELD AG, 1990, BIOCHEMISTRY-US, V29, P3509 REMAUT E, 1983, GENE, V22, P103 SARASTE M, 1990, TRENDS BIOCHEM SCI, V15, P430 SCHLICHTING I, 1990, NATURE, V345, P309 THOMPSON RC, 1988, TRENDS BIOCHEM SCI, V13, P91 TONG L, 1991, J MOL BIOL, V217, P503 WITTINGHOFER A, 1976, EUR J BIOCHEM, V62, P373 WOOLLEY P, 1989, BIO-TECHNOL, V7, P913 YAMASAKI K, 1989, BIOCHEM BIOPH RES CO, V162, P1054 |