1d7e

CRYSTAL STRUCTURE OF THE P65 CRYSTAL FORM OF PHOTOACTIVE YELLOW PROTEIN

spinqualitylabelsall models 1d7e, resolution 1.39Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1d7e is a 1 chain structure with sequence from Dsm 244. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HC4 Related: 2phy Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PYP_HALHA] Photoactive blue light protein. Probably functions as a photoreceptor for a negative phototaxis response. 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 PubMed The conformational changes during the photocycle of the photoactive yellow protein have been the subject of many recent studies. Spectroscopic measurements have shown that the photocycle also occurs in a crystalline environment, and this has been the basis for subsequent Laue diffraction and cryocrystallographic studies. These studies have shown that conformational changes during the photocycle are limited to the chromophore and its immediate environment. However, spectroscopic studies suggest the presence of large conformational changes in the protein. Here, we address this apparent discrepancy in two ways. First, we obtain a description of large concerted motions in the ground state of the yellow protein from NMR data and theoretical calculations. Second, we describe the high-resolution structure of the yellow protein crystallized in a different space group. The structure of the yellow protein differs significantly between the two crystal forms. We show that these differences can be used to obtain a description of the flexibility of the protein that is consistent with the motions observed in solution. Conformational substates in different crystal forms of the photoactive yellow protein--correlation with theoretical and experimental flexibility.,van Aalten DM, Crielaard W, Hellingwerf KJ, Joshua-Tor L Protein Sci. 2000 Jan;9(1):64-72. PMID:10739248 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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