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J Struct Funct Genomics. 2012 Mar;13(1):9-14. doi: 10.1007/s10969-011-9122-2. Epub 2011 Dec 24.

Solution NMR structures reveal a distinct architecture and provide first structures for protein domain family PF04536.

Author information

1
Department of Chemistry, The State University of New York at Buffalo, Buffalo, NY 14260, USA.

Abstract

The protein family (Pfam) PF04536 is a broadly conserved domain family of unknown function (DUF477), with more than 1,350 members in prokaryotic and eukaryotic proteins. High-quality NMR structures of the N-terminal domain comprising residues 41-180 of the 684-residue protein CG2496 from Corynebacterium glutamicum and the N-terminal domain comprising residues 35-182 of the 435-residue protein PG0361 from Porphyromonas gingivalis both exhibit an α/β fold comprised of a four-stranded β-sheet, three α-helices packed against one side of the sheet, and a fourth α-helix attached to the other side. In spite of low sequence similarity (18%) assessed by structure-based sequence alignment, the two structures are globally quite similar. However, moderate structural differences are observed for the relative orientation of two of the four helices. Comparison with known protein structures reveals that the α/β architecture of CG2496(41-180) and PG0361(35-182) has previously not been characterized. Moreover, calculation of surface charge potential and identification of surface clefts indicate that the two domains very likely have different functions.

PMID:
22198206
PMCID:
PMC3609422
DOI:
10.1007/s10969-011-9122-2
[Indexed for MEDLINE]
Free PMC Article

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