2pvb | pdb_00002pvb

PIKE PARVALBUMIN (PI 4.10) AT LOW TEMPERATURE (100K) AND ATOMIC RESOLUTION (0.91 A).

spinqualitylabelsall models 2pvb, resolution 0.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2pvb is a 1 chain structure with sequence from Esox lucius. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 0.91Å Ligands: ACE, CA, FMT, NH4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PRVB_ESOLU In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions. 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 Several crystal structures of parvalbumin (Parv), a typical EF-hand protein, have been reported so far for different species with the best resolution achieving 1.5 A. Using a crystal grown under microgravity conditions, cryotechniques (100 K), and synchrotron radiation, it has now been possible to determine the crystal structure of the fully Ca2+-loaded form of pike (component pI 4.10) Parv.Ca2 at atomic resolution (0.91 A). The availability of such a high quality structure offers the opportunity to contribute to the definition of the validation tools useful for the refinement of protein crystal structures determined to lower resolution. Besides a better definition of most of the elements in the protein three-dimensional structure than in previous studies, the high accuracy thus achieved allows the detection of well-defined alternate conformations, which are observed for 16 residues out of 107 in total. Among them, six occupy an internal position within the hydrophobic core and converge toward two small buried cavities with a total volume of about 60 A3. There is no indication of any water molecule present in these cavities. It is probable that at temperatures of physiological conditions there is a dynamic interconversion between these alternate conformations in an energy-barrier dependent manner. Such motions for which the amplitudes are provided by the present study will be associated with a time-dependent remodeling of the void internal space as part of a slow dynamics regime (millisecond timescales) of the parvalbumin molecule. The relevance of such internal dynamics to function is discussed. Crystal structure of the EF-hand parvalbumin at atomic resolution (0.91 A) and at low temperature (100 K). Evidence for conformational multistates within the hydrophobic core.,Declercq JP, Evrard C, Lamzin V, Parello J Protein Sci. 1999 Oct;8(10):2194-204. PMID:10548066 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Parvalbumin

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