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6M7M

rac-GSTSTA from degenerate octameric repeats in InaZ, residues 707-712

Summary for 6M7M
Entry DOI10.2210/pdb6m7m/pdb
Related6EEX
DescriptorL-GSTSTA from ice nucleation protein, inaZ, and its enantiomer, D-GSTSTA (2 entities in total)
Functional Keywordsamyloid, racemic, ice nucleation, microed, inaz, pseudomonas syringae, protein fibril
Biological sourcePseudomonas syringae
Total number of polymer chains1
Total formula weight522.51
Authors
Zee, C.,Glynn, C.,Gallagher-Jones, M.,Miao, J.,Santiago, C.G.,Cascio, D.,Gonen, T.,Sawaya, M.R.,Rodriguez, J.A. (deposition date: 2018-08-20, release date: 2019-04-03, Last modification date: 2024-03-13)
Primary citationZee, C.T.,Glynn, C.,Gallagher-Jones, M.,Miao, J.,Santiago, C.G.,Cascio, D.,Gonen, T.,Sawaya, M.R.,Rodriguez, J.A.
Homochiral and racemic MicroED structures of a peptide repeat from the ice-nucleation protein InaZ.
IUCrJ, 6:197-205, 2019
Cited by
PubMed Abstract: The ice-nucleation protein InaZ from contains a large number of degenerate repeats that span more than a quarter of its sequence and include the segment GSTSTA. structures of this repeat segment, resolved to 1.1 Å by microfocus X-ray crystallography and to 0.9 Å by the cryo-EM method MicroED, were determined from both racemic and homochiral crystals. The benefits of racemic protein crystals for structure determination by MicroED were evaluated and it was confirmed that the phase restriction introduced by crystal centrosymmetry increases the number of successful trials during the phasing of the electron diffraction data. Both homochiral and racemic GSTSTA form amyloid-like protofibrils with labile, corrugated antiparallel β-sheets that mate face to back. The racemic GSTSTA protofibril represents a new class of amyloid assembly in which all-left-handed sheets mate with their all-right-handed counterparts. This determination of racemic amyloid assemblies by MicroED reveals complex amyloid architectures and illustrates the racemic advantage in macromolecular crystallography, now with submicrometre-sized crystals.
PubMed: 30867917
DOI: 10.1107/S2052252518017621
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.101 Å)
Structure validation

226707

数据于2024-10-30公开中

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