3f1w

Crystal structure of a mutant proliferating cell nuclear antigen that blocks translesion synthesis

spinqualitylabelsall models 3f1w, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3f1w is a 1 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: POL30 (ATCC 18824) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PCNA_YEAST] This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Involved in DNA repair. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Proliferating cell nuclear antigen (PCNA) is a homotrimeric protein that functions as a sliding clamp during DNA replication. Several mutant forms of PCNA that block translesion DNA synthesis have been identified in genetic studies in yeast. One such mutant protein (encoded by the rev6-1 allele) is a glycine to serine substitution at residue 178, located at the subunit interface of PCNA. To improve our understanding of how this substitution interferes with translesion synthesis, we have determined the X-ray crystal structure of the PCNA G178S mutant protein. This substitution has little effect on the structure of the domain in which the substitution occurs. Instead, significant, local structural changes are observed in the adjacent subunit. The most notable difference between mutant and wild-type structures is in a single, extended loop (comprising amino acid residues 105-110), which we call loop J. In the mutant protein structure, loop J adopts a very different conformation in which the atoms of the protein backbone have moved by as much as 6.5 A from their positions in the wild-type structure. To improve our understanding of the functional consequences of this structural change, we have examined the ability of this mutant protein to stimulate nucleotide incorporation by DNA polymerase eta (pol eta). Steady state kinetic studies show that while wild-type PCNA stimulates incorporation by pol eta opposite an abasic site, the mutant PCNA protein actually inhibits incorporation opposite this DNA lesion. These results show that the position of loop J in PCNA plays an essential role in facilitating translesion synthesis. Structure of a mutant form of proliferating cell nuclear antigen that blocks translesion DNA synthesis.,Freudenthal BD, Ramaswamy S, Hingorani MM, Washington MT Biochemistry. 2008 Dec 16;47(50):13354-61. PMID:19053247 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Proliferating cell nuclear antigen 3D structures

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