Structural highlights
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.[1] [2] [3]
Publication Abstract from PubMed
X-ray structural determination of segments of the myosin rod has proved difficult because of the strong salt-dependent aggregation properties and repeating pattern of charges on the surface of the coiled-coil that lead to the formation of paracrystals. This problem has been resolved in part through the use of globular assembly domains that improve protein folding and prevent aggregation. The primary consideration now in designing coiled-coil fusion constructs for myosin is deciding where to truncate the coiled-coil and which amino acid residues to include from the folding domain. This is especially important for myosin that contains numerous regions of low predicted coiled-coil propensity. Here we describe the strategy adopted to determine the structure of the region that extends from Arg1677 - Leu1797 that included two areas that do not show a strong sequence signature of a conventional left-handed coiled coil or canonical heptad repeat. This demonstrates again that, with careful choice of fusion constructs, overlapping structures exhibit very similar conformations for the myosin rod fragments in the canonical regions. However, conformational variability is seen around Leu1706 which is a hot spot for cardiomyopathy mutations suggesting that this might be important for function.
Design Considerations in Coiled-Coil Fusion Constructs for the Structural Determination of a Problematic Region of the Human Cardiac Myosin Rod.,Andreas MP, Ajay G, Gellings JA, Rayment I J Struct Biol. 2017 Jul 22. pii: S1047-8477(17)30120-X. doi:, 10.1016/j.jsb.2017.07.006. PMID:28743637[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Choi KH, Morais MC, Anderson DL, Rossmann MG. Determinants of bacteriophage phi29 head morphology. Structure. 2006 Nov;14(11):1723-7. PMID:17098197 doi:http://dx.doi.org/10.1016/j.str.2006.09.007
- ↑ Fu CY, Morais MC, Battisti AJ, Rossmann MG, Prevelige PE Jr. Molecular dissection of o29 scaffolding protein function in an in vitro assembly system. J Mol Biol. 2007 Mar 2;366(4):1161-73. Epub 2006 Dec 6. PMID:17198713 doi:http://dx.doi.org/10.1016/j.jmb.2006.11.091
- ↑ Li R, Cherwa JE Jr, Prevelige PE Jr. varphi29 Scaffolding and connector structure-function relationship studied by trans-complementation. Virology. 2013 Sep;444(1-2):355-62. doi: 10.1016/j.virol.2013.07.001. Epub 2013, Jul 27. PMID:23896641 doi:http://dx.doi.org/10.1016/j.virol.2013.07.001
- ↑ Andreas MP, Ajay G, Gellings JA, Rayment I. Design Considerations in Coiled-Coil Fusion Constructs for the Structural Determination of a Problematic Region of the Human Cardiac Myosin Rod. J Struct Biol. 2017 Jul 22. pii: S1047-8477(17)30120-X. doi:, 10.1016/j.jsb.2017.07.006. PMID:28743637 doi:http://dx.doi.org/10.1016/j.jsb.2017.07.006
