2q4x
Ensemble refinement of the protein crystal structure of gene product from Arabidopsis thaliana At3g16990Ensemble refinement of the protein crystal structure of gene product from Arabidopsis thaliana At3g16990
Structural highlights
FunctionTENAE_ARATH Involved in thiamine salvage by hydrolyzing the thiamine breakdown product 4-amino-5-aminomethyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) (PubMed:25014715). Has a high formylamino-HMP amidohydrolase activity (PubMed:25014715). No activity with other thiamine degradation products such as thiamine mono- or diphosphate, oxothiamine, oxythiamine, thiamine disulfide, desthiothiamine or thiochrome as substrates (PubMed:25014715). Does not display thiaminase II activity, as it is unable to hydrolyze thiamine (PubMed:25014715). Is able to carry out two successive steps in the salvage of thiamine breakdown product, whereas two separate enzymes are required in Bacillus species (Probable). May also serve a damage pre-emption function by hydrolyzing products that would otherwise do harm (Probable).[1] [2] 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 PubMedX-ray crystallography typically uses a single set of coordinates and B factors to describe macromolecular conformations. Refinement of multiple copies of the entire structure has been previously used in specific cases as an alternative means of representing structural flexibility. Here, we systematically validate this method by using simulated diffraction data, and we find that ensemble refinement produces better representations of the distributions of atomic positions in the simulated structures than single-conformer refinements. Comparison of principal components calculated from the refined ensembles and simulations shows that concerted motions are captured locally, but that correlations dissipate over long distances. Ensemble refinement is also used on 50 experimental structures of varying resolution and leads to decreases in R(free) values, implying that improvements in the representation of flexibility observed for the simulated structures may apply to real structures. These gains are essentially independent of resolution or data-to-parameter ratio, suggesting that even structures at moderate resolution can benefit from ensemble refinement. Ensemble refinement of protein crystal structures: validation and application.,Levin EJ, Kondrashov DA, Wesenberg GE, Phillips GN Jr Structure. 2007 Sep;15(9):1040-52. PMID:17850744[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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