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NMR structure of the Bordetella bronchiseptica protein NP_888769.1 establishes a new phage‐related protein family PF13554
Author(s) -
Wahab Atiatul,
Serrano Pedro,
Geralt Michael,
Wüthrich Kurt
Publication year - 2011
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.641
Subject(s) - antiparallel (mathematics) , structural genomics , bordetella bronchiseptica , prophage , homology (biology) , genetics , biology , bordetella , homology modeling , protein structure , bacteriophage , genome , peptide sequence , computational biology , structural alignment , sequence alignment , gene , biochemistry , bacteria , physics , escherichia coli , bordetella pertussis , quantum mechanics , magnetic field , enzyme
Abstract The solution structure of the hypothetical phage‐related protein NP_888769.1 from the Gram‐negative bacterium Bordetella bronchoseptica contains a well‐structured core comprising a five‐stranded, antiparallel β‐sheet packed on one side against two α‐helices and a short β‐hairpin with three flexibly disordered loops extending from the central β‐sheet. A homology search with the software DALI identified two Protein Data Bank deposits with Z‐scores > 8, where both of these proteins have less than 8% sequence identity relative to NP_888769.1, and one has been functionally annotated as a lambda phage tail terminator protein. A sequence‐homology analysis then confirmed that NP_888769.1 represents the first three‐dimensional structural representative of a new protein family that was previously predicted by the Joint Center for Structural Genomics, which includes so far about 20 prophage proteins encoded in bacterial genomes.