3h8y
From Proteopedia
Crystal structure of carboxysome small shell protein CsoS1C from Halothiobacillus neapolitanus
Structural highlights
FunctionCSOSC_HALNC One of shell proteins of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, ccbL-ccbS) is sequestered. Assembles into hexamers which make sheets that form the facets of the polyhedral carboxysome (Probable). The shell probably limits the diffusion of CO(2) into and out of the carboxysome (Probable). There are estimated to be 2970 CsoS1A/CsoS1C proteins per carboxysome (the proteins differ by only 1 residue) (Ref.4).[1] [2] [3] Unlike beta-carboxysomes, alpha-carboxysomes (Cb) can form without cargo protein. CsoS2 is essential for Cb formation and is also capable of targeting foreign proteins to the Cb. The Cb shell assembles with the aid of CsoS2; CsoS1A, CsoS1B and CsoS1C form the majority of the shell while CsoS4A and CsoS4B form vertices. CsoS1D forms pseudohexamers that probably control metabolite flux into and out of the shell.[4] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedLattice-translocation or crystal order-disorder phenomena occur when some layers or groups of molecules in a crystal are randomly displaced relative to other groups of molecules by a discrete set of vectors. In previous work, the effects of lattice translocation on diffraction intensities have been corrected by considering that the observed intensities are the product of the intensities from an ideal crystal (lacking disorder) multiplied by the squared magnitude of the Fourier transform of the set of translocation vectors. Here, the structure determination is presented of carboxysome protein CsoS1C from Halothiobacillius neapolitanus in a crystal exhibiting a lattice translocation with unique features. The diffraction data are fully accounted for by a crystal unit cell composed of two layers of cyclic protein hexamers. The first layer is fully ordered (i.e. has one fixed position), while the second layer randomly takes one of three alternative positions whose displacements are related to each other by threefold symmetry. Remarkably, the highest symmetry present in the crystal is P3, yet the intensity data (and the Patterson map) obey 6/m instead of \overline 3 symmetry; the intensities exceed the symmetry expected from combining the crystal space group with an inversion center. The origin of this rare phenomenon, known as symmetry enhancement, is discussed and shown to be possible even for a perfectly ordered crystal. The lattice-translocation treatment described here may be useful in analyzing other cases of disorder in which layers or groups of molecules are shifted in multiple symmetry-related directions. Analysis of lattice-translocation disorder in the layered hexagonal structure of carboxysome shell protein CsoS1C.,Tsai Y, Sawaya MR, Yeates TO Acta Crystallogr D Biol Crystallogr. 2009 Sep;65(Pt 9):980-8. Epub 2009, Aug 14. PMID:19690376[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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