4nyq | pdb_00004nyq

In-vivo crystallisation (midguts of a viviparous cockroach) and structure at 1.2 A resolution of a glycosylated, lipid-binding, lipocalin-like protein

spinqualitylabelsall models 4nyq, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4nyq is a 1 chain structure with sequence from Diploptera punctata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.2Å Ligands: BMA, EIC, GOL, NAG, OLA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6SVB6_DIPPU Publication Abstract from PubMed Macromolecular crystals for X-ray diffraction studies are typically grown in vitro from pure and homogeneous samples; however, there are examples of protein crystals that have been identified in vivo. Recent developments in micro-crystallography techniques and the advent of X-ray free-electron lasers have allowed the determination of several protein structures from crystals grown in cellulo. Here, an atomic resolution (1.2 A) crystal structure is reported of heterogeneous milk proteins grown inside a living organism in their functional niche. These in vivo-grown crystals were isolated from the midgut of an embryo within the only known viviparous cockroach, Diploptera punctata. The milk proteins crystallized in space group P1, and a structure was determined by anomalous dispersion from the native S atoms. The data revealed glycosylated proteins that adopt a lipocalin fold, bind lipids and organize to form a tightly packed crystalline lattice. A single crystal is estimated to contain more than three times the energy of an equivalent mass of dairy milk. This unique storage form of nourishment for developing embryos allows access to a constant supply of complete nutrients. Notably, the crystalline cockroach-milk proteins are highly heterogeneous with respect to amino-acid sequence, glycosylation and bound fatty-acid composition. These data present a unique example of protein heterogeneity within a single in vivo-grown crystal of a natural protein in its native environment at atomic resolution. Structure of a heterogeneous, glycosylated, lipid-bound, in vivo-grown protein crystal at atomic resolution from the viviparous cockroach Diploptera punctata.,Banerjee S, Coussens NP, Gallat FX, Sathyanarayanan N, Srikanth J, Yagi KJ, Gray JS, Tobe SS, Stay B, Chavas LM, Ramaswamy S IUCrJ. 2016 Jun 27;3(Pt 4):282-93. doi: 10.1107/S2052252516008903. eCollection, 2016 Jul 1. PMID:27437115 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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