3oa7 | pdb_00003oa7

Structure of the C-terminal domain of Cnm67, a core component of the spindle pole body of Saccharomyces cerevisiae

spinqualitylabelsall models 3oa7, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3oa7 is a 1 chain structure with sequence from Bacillus virus phi29 and Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SCAF_BPPH2 Scaffolding protein involved in the icosahedric procapsid assembly. Coassembles with the capsid proteins to form the procapsid, in which the scaffolding protein is found within the external shell of icosahedrally arranged capsid protein subunits. In a subsequent step the scaffolding protein molecules are released from the procapsid. CNM67_YEAST Involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation. Required for the proper formation of the spindle pole body (SPB) outer plaque. May connect the outer plaque to the central plaque embedded in the nuclear envelope. Publication Abstract from PubMed The spindle pole body of the budding yeast Saccharomyces cerevisiae has served as a model system for understanding microtubule organizing centers, yet very little is known about the molecular structure of its components. We report here the structure of the C-terminal domain of the core component Cnm67 at 2.3 A resolution. The structure determination was aided by a novel approach to crystallization of proteins containing coiled-coils that utilizes globular domains to stabilize the coiled-coils. This enhances their solubility in Escherichia coli and improves their crystallization. The Cnm67 C-terminal domain (residues Asn-429-Lys-581) exhibits a previously unseen dimeric, interdigitated, all alpha-helical fold. In vivo studies demonstrate that this domain alone is able to localize to the spindle pole body. In addition, the structure reveals a large functionally indispensable positively charged surface patch that is implicated in spindle pole body localization. Finally, the C-terminal eight residues are disordered but are critical for protein folding and structural stability. Structure-function analysis of the C-terminal domain of CNM67, a core component of the Saccharomyces cerevisiae spindle pole body.,Klenchin VA, Frye JJ, Jones MH, Winey M, Rayment I J Biol Chem. 2011 May 20;286(20):18240-50. Epub 2011 Mar 24. PMID:21454609 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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