2l3u | pdb_00002l3u

Solution Structure of Domain IV from the YbbR family protein of Desulfitobacterium hafniense: Northeast Structural Genomics Consortium target DhR29A

spinqualitylabelsall models 2l3u, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2l3u is a 1 chain structure with sequence from Deshd. This structure supersedes the now removed PDB entry 2kps. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: Dhaf_0833 (DESHD) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 YbbR domains are widespread throughout Eubacteria and are expressed as monomeric units, linked in tandem repeats or cotranslated with other domains. Although the precise role of these domains remains undefined, the location of the multiple YbbR domain-encoding ybbR gene in the Bacillus subtilis glmM operon and its previous identification as a substrate for a surfactin-type phosphopantetheinyl transferase suggests a role in cell growth, division, and virulence. To further characterize the YbbR domains, structures of two of the four domains (I and IV) from the YbbR-like protein of Desulfitobacterium hafniense Y51 were solved by solution nuclear magnetic resonance and X-ray crystallography. The structures show the domains to have nearly identical topologies despite a low amino acid identity (23%). The topology is dominated by beta-strands, roughly following a "figure 8" pattern with some strands coiling around the domain perimeter and others crossing the center. A similar topology is found in the C-terminal domain of two stress-responsive bacterial ribosomal proteins, TL5 and L25. Based on these models, a structurally guided amino acid alignment identifies features of the YbbR domains that are not evident from naive amino acid sequence alignments. A structurally conserved cis-proline (cis-Pro) residue was identified in both domains, though the local structure in the immediate vicinities surrounding this residue differed between the two models. The conservation and location of this cis-Pro, plus anchoring Val residues, suggest this motif may be significant to protein function. Structures of domains I and IV from YbbR are representative of a widely distributed protein family.,Barb AW, Cort JR, Seetharaman J, Lew S, Lee HW, Acton T, Xiao R, Kennedy MA, Tong L, Montelione GT, Prestegard JH Protein Sci. 2011 Feb;20(2):396-405. doi: 10.1002/pro.571. Epub 2011 Jan, 18. PMID:21154411 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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