Functional fragments of disorder in outer membrane β barrel proteins

Intrinsically Disordered Proteins
Kavitha KurupSankaran Krishnaswamy

Abstract

The traditional view of "sequence-structure-function" has been amended by the discovery of intrinsically disordered proteins. Almost 50% of PDB structures are now known to have one or more regions of disorder, which are involved in diverse functions. These regions typically possess low aromatic content and sequence complexity as well as high net charge and flexibility. In this study, we examined the composition and contribution of intrinsic disorder in outer membrane β barrel protein functions. Our systematic analysis to find the dual personality (DP) fragments, which often function by disorder-order transitions, revealed the presence of 61 DP fragments with 234 residues in β barrel trans membrane protein structures. It was found that though the disorder is more prevalent in the periplasmic regions, most of the residues which undergo disorder-order transitions are found in the extracellular regions. For example, the calcium binding sites in BtuB protein are found to undergo disorder to order transition upon binding calcium. The conformational change in the cell receptor binding site of the OpcA protein, which is important in host cell interactions of N. meningitidis, was also found to be due to the disorder-order transitions oc...Continue Reading

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Citations

Jun 12, 2017·Cellular and Molecular Life Sciences : CMLS·Magnus Kjaergaard, Birthe B Kragelund
Nov 7, 2018·Journal of Molecular Recognition : JMR·Konda Mani Saravanan, Karthe Ponnuraj

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Methods Mentioned

BETA
X-ray

Software Mentioned

Scansite
PYMOL
Jalview
Superpose
BLAST
XML2PDB
Generalized Association Plot ( GAP )
Composition Profiler
GAP
TMBETA

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