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1ZDK

STRUCTURE OF BACTERIOPHAGE COAT PROTEIN-LOOP RNA COMPLEX

Summary for 1ZDK
Entry DOI10.2210/pdb1zdk/pdb
DescriptorRNA (5'-R(P*AP*CP*AP*UP*GP*AP*GP*GP*AP*UP*CP*AP*CP*CP*CP*AP*UP*GP*U)-3'), PROTEIN (MS2 PROTEIN CAPSID) (3 entities in total)
Functional Keywordscomplex (coat protein-rna), coat protein, rna-binding, viral protein capsid, rna fragment, icosahedral virus, virus-rna complex, virus/rna
Biological sourceEnterobacterio phage MS2
More
Cellular locationVirion (Potential): P03612
Total number of polymer chains5
Total formula weight53338.74
Authors
Grahn, E.,Stonehouse, N.J.,Valegard, K.,Vandenworm, S.,Liljas, L. (deposition date: 1998-12-04, release date: 1998-12-07, Last modification date: 2024-05-22)
Primary citationGrahn, E.,Stonehouse, N.J.,Murray, J.B.,van den Worm, S.,Valegard, K.,Fridborg, K.,Stockley, P.G.,Liljas, L.
Crystallographic studies of RNA hairpins in complexes with recombinant MS2 capsids: implications for binding requirements.
RNA, 5:131-138, 1999
Cited by
PubMed Abstract: The coat protein of bacteriophage MS2 is known to bind specifically to an RNA hairpin formed within the MS2 genome. Structurally this hairpin is built up by an RNA double helix interrupted by one unpaired nucleotide and closed by a four-nucleotide loop. We have performed crystallographic studies of complexes between MS2 coat protein capsids and four RNA hairpin variants in order to evaluate the minimal requirements for tight binding to the coat protein and to obtain more information about the three-dimensional structure of these hairpins. An RNA fragment including the four loop nucleotides and a two-base-pair stem but without the unpaired nucleotide is sufficient for binding to the coat protein shell under the conditions used in this study. In contrast, an RNA fragment containing a stem with the unpaired nucleotide but missing the loop nucleotides does not bind to the protein shell.
PubMed: 9917072
DOI: 10.1017/S1355838299981645
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.86 Å)
Structure validation

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数据于2024-10-30公开中

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