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Structure of BT_3984, a member of the SusD/RagB family of nutrient-binding molecules

Academic Article
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Overview

authors

  • Bakolitsa, C.
  • Xu, Q. P.
  • Rife, C. L.
  • Abdubek, P.
  • Astakhova, T.
  • Axelrod, H. L.
  • Carlton, D.
  • Chen, C.
  • Chiu, H. J.
  • Clayton, T.
  • Das, D.
  • Deller, M. C.
  • Duan, L. A.
  • Ellrott, K.
  • Farr, C. L.
  • Feuerhelm, J.
  • Grant, J. C.
  • Grzechnik, A.
  • Han, G. W.
  • Jaroszewski, L.
  • Jin, K. K.
  • Klock, H. E.
  • Knuth, M. W.
  • Kozbial, P.
  • Krishna, S. S.
  • Kumar, A.
  • Lam, W. W.
  • Marciano, David
  • McMullan, D.
  • Miller, M. D.
  • Morse, A. T.
  • Nigoghossian, E.
  • Nopakun, A.
  • Okach, L.
  • Puckett, C.
  • Reyes, R.
  • Tien, H. J.
  • Trame, C. B.
  • van den Bedem, H.
  • Weekes, D.
  • Hodgson, K. O.
  • Wooley, J.
  • Elsliger, M. A.
  • Deacon, A. M.
  • Godzik, A.
  • Lesley, Scott
  • Wilson, Ian

publication date

  • October 2010

journal

  • Acta Crystallographica Section F-Structural Biology and Crystallization Communications  Journal

abstract

  • The crystal structure of the Bacteroides thetaiotaomicron protein BT_3984 was determined to a resolution of 1.7?? and was the first structure to be determined from the extensive SusD family of polysaccharide-binding proteins. SusD is an essential component of the sus operon that defines the paradigm for glycan utilization in dominant members of the human gut microbiota. Structural analysis of BT_3984 revealed an N-terminal region containing several tetratricopeptide repeats (TPRs), while the signature C-terminal region is less structured and contains extensive loop regions. Sequence and structure analysis of BT_3984 suggests the presence of binding interfaces for other proteins from the polysaccharide-utilization complex.
  • The crystal structure of the Bacteroides thetaiotaomicron protein BT_3984 was determined to a resolution of 1.7 Å and was the first structure to be determined from the extensive SusD family of polysaccharide-binding proteins. SusD is an essential component of the sus operon that defines the paradigm for glycan utilization in dominant members of the human gut microbiota. Structural analysis of BT_3984 revealed an N-terminal region containing several tetratricopeptide repeats (TPRs), while the signature C-terminal region is less structured and contains extensive loop regions. Sequence and structure analysis of BT_3984 suggests the presence of binding interfaces for other proteins from the polysaccharide-utilization complex.

subject areas

  • Amino Acid Sequence
  • Bacterial Proteins
  • Bacteroides
  • Crystallography, X-Ray
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Structural Homology, Protein
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Identity

PubMed Central ID

  • PMC2954216

International Standard Serial Number (ISSN)

  • 1744-3091

Digital Object Identifier (DOI)

  • 10.1107/s1744309110032999

PubMed ID

  • 20944222
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Additional Document Info

start page

  • 1274

end page

  • 1280

volume

  • 66

issue

  • Pt 10

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