Figure 23.3.4.7

Dickerson, R. E.

doi:10.1107/97809553602060000716

International
Tables for
Crystallography
Volume F
Crystallography of biological macromolecules
Edited by M. G. Rossmann and E. Arnold

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International Tables for Crystallography (2006). Vol. F. ch. 23.3, p. 606 | 1 | 2 |

Figure 23.3.4.7

R. E. Dickerson^a ^*

^a Molecular Biology Institute, University of California, Los Angeles, Los Angeles, CA 90095–1570, USA
Correspondence e-mail: red@mbi.ucla.edu

Figure 23.3.4.7

Bending via roll at T-A steps in TBP or the TATA-binding protein (top) and in γδ-resolvase (bottom). Note that not every T-A step in TBP or γδ-resolvase is necessarily bent. Note also in γδ-resolvase that C-A = T-G steps, which in proteins such as CAP are used to generate sharp roll bends, here, frequently, are local roll maxima, even though they contribute little to the overall bending. They have a bending potential that is not used in this particular setting.