2d6b
From Proteopedia
Novel Bromate Species trapped within a Protein Crystal
Structural highlights
Function[LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.[1] 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 PubMedOnly a few protein-oxoanion crystal complexes have been described to date. Here, the structure of a protein soaked in a bromate solution has been determined to a resolution of 1.25 A and refined to final overall R/R(free) values of 18.04/21.3 (isotropic) and 11.25/14.67 (anisotropic). In contrast to the single-model approach, refinement of an ensemble of ten models enabled us to determine variances and statistically evaluate bond-length distances and angles in the oxoanions. In total, nine bromate positions, including two BrO(3)(-) x HBrO(3) dimer species, have been identified on the basis of the anomalous signal of the Br atoms. For all bromate ions, the main-chain amide atoms of the protein were identified as the dominant binding positions, a useful property in any experimental phase-determination experiment. An ensemble of crystallographic models enables the description of novel bromate-oxoanion species trapped within a protein crystal.,Ondracek J, Mesters JR Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):996-1001. Epub 2006, Aug 19. PMID:16929100[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Chick | Large Structures | Lysozyme | Mesters, J R | Ondracek, J | Bromate | Hydrolase
