2OJ5

Crystal Structure of Reovirus T3D Attachment Protein Sigma1 head domain wild-type at 1.75 A resolution

Summary for 2OJ5

• Entry DOI: 10.2210/pdb2oj5/pdb
• Related: 1KKE 2OJ6
• Descriptor: Viral attachment protein sigma 1, MAGNESIUM ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: beta-barrel, beta-spiral repeat, aspartic acid cluster, greek key motif, trimer, viral protein
• Biological source: Reovirus sp.
• Total number of polymer chains: 6
• Total formula weight: 107642.60

Authors

Stehle, T.,Schelling, P.,Kirchner, E.,Dermody, T.S. (deposition date: 2007-01-12, release date: 2007-02-13, Last modification date: 2023-08-30)

Primary citation

Schelling, P.,Guglielmi, K.M.,Kirchner, E.,Paetzold, B.,Dermody, T.S.,Stehle, T.
The Reovirus Sigma1 Aspartic Acid Sandwich: A TRIMERIZATION MOTIF POISED FOR CONFORMATIONAL CHANGE.
J.Biol.Chem., 282:11582-11589, 2007

PubMed Abstract: Reovirus attachment protein sigma1 mediates engagement of receptors on the surface of target cells and undergoes dramatic conformational rearrangements during viral disassembly in the endocytic pathway. The sigma1 protein is a filamentous, trimeric molecule with a globular beta-barrel head domain. An unusual cluster of aspartic acid residues sandwiched between hydrophobic tyrosines is located at the sigma1 subunit interface. A 1.75-A structure of the sigma1 head domain now reveals two water molecules at the subunit interface that are held strictly in position and interact with neighboring residues. Structural and biochemical analyses of mutants affecting the aspartic acid sandwich indicate that these residues and the corresponding chelated water molecules act as a plug to block the free flow of solvent and stabilize the trimer. This arrangement of residues at the sigma1 head trimer interface illustrates a new protein design motif that may confer conformational mobility during cell entry.

PubMed: 17303562
DOI: 10.1074/jbc.M610805200

Experimental method

X-RAY DIFFRACTION (1.75 Å)