TY - JOUR
T1 - The crystal structure of d(Ccccgggg)
T2 - A new a-form variant with an extended backbone conformation
AU - Haran, T. E.
AU - Shakked, Z.
AU - Wang, A. H.
AU - Rich, A.
PY - 1987/10
Y1 - 1987/10
N2 - The crystal structure of d(CCCCGGGG) has been determined at a resolution of 2.25Ȧ. The oligomers crystallize as A-DNA duplexes occupying crystallographic two-fold axes. The backbone conformation is, in general, similar to that observed in previously reported crystal structures of A-DNA fragments, except for the central linkage, where it adopts an extended structure resulting from all trans conformation at the P-05’-C5’-C4′ bonds. This type of conformation facilitates interstrand stacking between the guanines at the C-G site. The local helix twist at this step is very small (25°) compared to an overall average of 33.5°. The unique structure of the C-G base-pair step, namely the extended backbone and the distinct stacking geometry, may be an important feature in the recognition mechanism between doublestranded DNA molecules and restriction endonucleases such as Msp I, which cuts the sequence CCGG very specifically with a rate unaffected by neighboring base pairs.
AB - The crystal structure of d(CCCCGGGG) has been determined at a resolution of 2.25Ȧ. The oligomers crystallize as A-DNA duplexes occupying crystallographic two-fold axes. The backbone conformation is, in general, similar to that observed in previously reported crystal structures of A-DNA fragments, except for the central linkage, where it adopts an extended structure resulting from all trans conformation at the P-05’-C5’-C4′ bonds. This type of conformation facilitates interstrand stacking between the guanines at the C-G site. The local helix twist at this step is very small (25°) compared to an overall average of 33.5°. The unique structure of the C-G base-pair step, namely the extended backbone and the distinct stacking geometry, may be an important feature in the recognition mechanism between doublestranded DNA molecules and restriction endonucleases such as Msp I, which cuts the sequence CCGG very specifically with a rate unaffected by neighboring base pairs.
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U2 - 10.1080/07391102.1987.10506390
DO - 10.1080/07391102.1987.10506390
M3 - Article
C2 - 3271472
AN - SCOPUS:0023423118
SN - 0739-1102
VL - 5
SP - 199
EP - 218
JO - Journal of Biomolecular Structure and Dynamics
JF - Journal of Biomolecular Structure and Dynamics
IS - 2
ER -