-
19
-
-
0032724654
-
-
I. S. Ridder, H. J. Rozeboom, K. H. Kalk, B. W. Dijkstra, J. Biol. Chem. 274, 30672 (1999).
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 30672
-
-
Ridder, I.S.1
Rozeboom, H.J.2
Kalk, K.H.3
Dijkstra, B.W.4
-
21
-
-
0032510685
-
-
H. Kack, K. J. Gibson, Y. Lindqvist, G. Schneider, Proc. Natl. Acad. Sci. U.S.A. 95, 5495 (1998).
-
(1998)
Proc. Natl. Acad. Sci. U.S.A.
, vol.95
, pp. 5495
-
-
Kack, H.1
Gibson, K.J.2
Lindqvist, Y.3
Schneider, G.4
-
22
-
-
0035850820
-
-
A. Heine et al., Science 294, 369 (2001).
-
(2001)
Science
, vol.294
, pp. 369
-
-
Heine, A.1
-
24
-
-
0029931810
-
-
M. J. Brubaker, D. H. Dyer, B. Stoddard, D. E. Koshland Jr., Biochemistry 35, 2854 (1996).
-
(1996)
Biochemistry
, vol.35
, pp. 2854
-
-
Brubaker, M.J.1
Dyer, D.H.2
Stoddard, B.3
Koshland D.E., Jr.4
-
26
-
-
0028021801
-
-
N. Qian, G. A. Stanley, B. Hahn-Hagerdal, P. Radstrom, J. Bacteriol. 176, 5304 (1994).
-
(1994)
J. Bacteriol.
, vol.176
, pp. 5304
-
-
Qian, N.1
Stanley, G.A.2
Hahn-Hagerdal, B.3
Radstrom, P.4
-
27
-
-
0037165383
-
-
R. E. Hanes Jr., V. M. Lynch, E. V. Anslyn, K. N. Dalby, Org. Lett. 4, 201 (2001).
-
(2001)
Org. Lett.
, vol.4
, pp. 201
-
-
Hanes R.E., Jr.1
Lynch, V.M.2
Anslyn, E.V.3
Dalby, K.N.4
-
28
-
-
0026664620
-
-
J. B. Dai, Y. Liu, W. J. Ray Jr., M. Konno, J. Biol. Chem. 267, 6322 (1992).
-
(1992)
J. Biol. Chem.
, vol.267
, pp. 6322
-
-
Dai, J.B.1
Liu, Y.2
Ray W.J., Jr.3
Konno, M.4
-
29
-
-
1842368457
-
-
N. Qian, G. A. Stanley, A. Bunte, P. Radstrom, Microbiology 143 (Pt 3), 855 (1997).
-
(1997)
Microbiology
, vol.143
, Issue.PART 3
, pp. 855
-
-
Qian, N.1
Stanley, G.A.2
Bunte, A.3
Radstrom, P.4
-
32
-
-
0037008092
-
-
S. D. Lahiri, G. Zhang, D. Dunaway-Mariano, K. N. Allen, Biochemistry 41, 8351 (2002).
-
(2002)
Biochemistry
, vol.41
, pp. 8351
-
-
Lahiri, S.D.1
Zhang, G.2
Dunaway-Mariano, D.3
Allen, K.N.4
-
34
-
-
0242472865
-
-
note
-
In earlier work, β-PGM was isolated from the cell in its phosphorylated form and crystallized in the presence of its Mg(II) cofactor for structure determination (32). Overall, β-PGM is a monomer that is composed of two distinct domains: a helical cap domain and an α/β core domain. Whereas the conformations of individual domains of the phosphorylated enzyme-Mg(II) complex and the enzyme-Mg(11)-β-P-G1,6-P complexes are nearly indistinguishable, the positions of the cap domains relative to the core domains are noticeably different. A hinge-like motion between the two domains, acting as rigid bodies, produces the conversion of one enzyme conformer to the other, enveloping the β-G1,6-P intermediate.
-
-
-
-
35
-
-
2142803437
-
-
Materials and methods are available as supporting material on Science Online.
-
Science Online
-
-
-
45
-
-
0242556515
-
-
note
-
Hydrogen bonds are made between the C(6)phosphal:e and the N118 side chain NH2, S116 side chain OH, K117 amide NH, the two R49 guanidinium NHs, Wat 231, Wat 48, Wat5, Wat129; hexose C(4)O and Wat129 and V47 amide NH; hexose C(3)O and Wat68; C(2)O and Wats68 and 29; and hexose C(5)O and S116 amide NH.
-
-
-
-
46
-
-
0242556514
-
-
note
-
For this analysis, the model of the ligand β-G1,6-P was refined in a crystallography and nuclear magnetic resonance system with geometric constraints for normal tetrahedral hybridization at phosphorus during the initial stages of refinement of the 1.2 Å structure. The model of the ligand was docked into the active site by overlaying the hexose ring, C(6)phosphate, and C(1)phosphate phosphorus portion of the molecule with that of the pentavalent intermediate.
-
-
-
-
48
-
-
0026655361
-
-
A. L Morris, M. W. MacArthur, E. G. Hutchinson, J. M. Thornton, Proteins 12, 345 (1992).
-
(1992)
Proteins
, vol.12
, pp. 345
-
-
Morris, A.L.1
MacArthur, M.W.2
Hutchinson, E.G.3
Thornton, J.M.4
-
49
-
-
0242389514
-
-
note
-
Supported by a grant from NIH (grant GM16099) (to K.N.A and D.D-.M). Use of the Advanced Photon Source was supported by the U.S. Department of Energy, Basic Energy Sciences, Office of Science, under contract no. W-31-109-Eng-38. Use of the BioCARS Sector 14 was supported by NIH, National Center for Research Resources, under grant number RR07707. Research was carried out (in part) at the HHMI beamline X4A at the National Synchrotron Light Source, Brookhaven National Laboratory. Coordinates have been deposited in the Protein Data Bank (accession codes 1O08 and 1O03, for G1P and G6P cocrystals, respectively). We thank W. W. Cleland, G. Petsko, D. Ringe, R. Holmes, and A. Mildvan for careful reading of the manuscript, and E. Peisach for his generous help with graphics.
-
-
-
|