1sty | pdb_00001sty

THE ALPHA ANEURISM: A STRUCTURAL MOTIF REVEALED IN AN INSERTION MUTANT OF STAPHYLOCOCCAL NUCLEASE

spinqualitylabelsall models 1sty, resolution 1.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1sty is a 1 chain structure with sequence from "micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, THP Activity: Micrococcal nuclease, with EC number 3.1.31.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [NUC_STAAU] Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond. 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 The x-ray crystal structure of a mutant of staphylococcal nuclease that contains a single glycine residue inserted in the C-terminal alpha-helix has been solved to 1.67 A resolution and refined to a crystallographic R value of 0.170. This inserted glycine residue is accommodated in the alpha-helix by formation of a previously uncharacterized bulge, which we term the alpha aneurism. A conformational search of known protein structures has identified the alpha aneurism in a number of protein families, including the histocompatibility antigens and hemoglobins. The alpha aneurism: a structural motif revealed in an insertion mutant of staphylococcal nuclease.,Keefe LJ, Sondek J, Shortle D, Lattman EE Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3275-9. PMID:8475069 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Staphylococcal nuclease

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