4kyc

Structure of the C-terminal domain of the Menangle virus phosphoprotein, fused to MBP.

spinqualitylabelsall models 4kyc, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4kyc is a 1 chain structure with sequence from Escherichia coli K-12 and Menangle virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BO3, EDO, GLC, PRD_900001 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.Q91MK1_9MONO Essential component of the RNA polymerase and the nascent chain assembly complex. Also required during RNA synthesis.[ARBA:ARBA00002047] Publication Abstract from PubMed Proteins are often classified in a binary fashion as either structured or disordered. However this approach has several deficits. Firstly, protein folding is always conditional on the physiochemical environment. A protein which is structured in some circumstances will be disordered in others. Secondly, it hides a fundamental asymmetry in behavior. While all structured proteins can be unfolded through a change in environment, not all disordered proteins have the capacity for folding. Failure to accommodate these complexities confuses the definition of both protein structural domains and intrinsically disordered regions. We illustrate these points with an experimental study of a family of small binding domains, drawn from the RNA polymerase of mumps virus and its closest relatives. Assessed at face value the domains fall on a structural continuum, with folded, partially folded, and near unstructured members. Yet the disorder present in the family is conditional, and these closely related polypeptides can access the same folded state under appropriate conditions. Any heuristic definition of the protein domain emphasizing conformational stability divides this domain family in two, in a way that makes no biological sense. Structural domains would be better defined by their ability to adopt a specific tertiary structure: a structure that may or may not be realized, dependent on the circumstances. This explicitly allows for the conditional nature of protein folding, and more clearly demarcates structural domains from intrinsically disordered regions that may function without folding. Protein domain definition should allow for conditional disorder.,Yegambaram K, Bulloch EM, Kingston RL Protein Sci. 2013 Aug 20. doi: 10.1002/pro.2336. PMID:23963781 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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