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"Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP." |
Ollis DL, Brick P, Hamlin R, Xuong NG, Steitz TA |
Published Jan. 1, 1985 in Nature volume 313 .
Pubmed ID: 3883192
Abstract:
| The 3.3-A resolution crystal structure of the large proteolytic fragment of Escherichia coli DNA polymerase I complexed with deoxythymidine monophosphate consists of two domains, the smaller of which binds zinc-deoxythymidine monophosphate. The most striking feature of the larger domain is a deep crevice of the appropriate size and shape for binding double-stranded B-DNA. A flexible subdomain may allow the enzyme to surround completely the DNA substrate, thereby allowing processive nucleotide polymerization without enzyme dissociation. |
This publication refers to following REPAIRtoire entries:
| Proteins |
Last modification of this entry: Oct. 6, 2010
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