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

Journal Article · · Acta Crystallographica. Section F
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  1. Joint Center for Structural Genomics, http://www.jcsg.org (United States); Sanford–Burnham Medical Research Inst., La Jolla, CA (United States). Program on Bioinformatics and Systems Biology
  2. Joint Center for Structural Genomics, http://www.jcsg.org (United States); SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
  3. Joint Center for Structural Genomics, http://www.jcsg.org (United States); Genomics Institute of the Novartis Research Foundation, San Diego, CA (United States). Protein Sciences Dept.
  4. Joint Center for Structural Genomics, http://www.jcsg.org (United States); Univ. of California, San Diego, La Jolla, CA (United States). Center for Research in Biological Systems
  5. Joint Center for Structural Genomics, http://www.jcsg.org (United States); The Scripps Research Inst., La Jolla, CA (United States). Dept. of Molecular Biology
  6. Joint Center for Structural Genomics, http://www.jcsg.org (United States); Sanford–Burnham Medical Research Inst., La Jolla, CA (United States). Program on Bioinformatics and Systems Biology; Univ. of California, San Diego, La Jolla, CA (United States). Center for Research in Biological Systems
  7. Joint Center for Structural Genomics, http://www.jcsg.org (United States); SLAC National Accelerator Lab., Menlo Park, CA (United States). Photon Science
  8. Joint Center for Structural Genomics, http://www.jcsg.org (United States); Genomics Institute of the Novartis Research Foundation, San Diego, CA (United States). Protein Sciences Dept.; The Scripps Research Inst., La Jolla, CA (United States). Dept. of Molecular Biology
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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.

Research Organization:
SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
Sponsoring Organization:
USDOE Office of Science (SC), Biological and Environmental Research (BER); National Institutes of Health (NIH); National Institute of General Medical Sciences (NIGMS); National Center for Research Resources (NCRR); USDOE Office of Science (SC), Basic Energy Sciences (BES)
Grant/Contract Number:
AC02-76SF00515; U54 GM074898
OSTI ID:
1625804
Journal Information:
Acta Crystallographica. Section F, Vol. 66, Issue 10; ISSN 1744-3091
Publisher:
International Union of CrystallographyCopyright Statement
Country of Publication:
United States
Language:
English

Cited By (1)

Structure of RagB, a major immunodominant outer-membrane surface receptor antigen of Porphyromonas gingivalis journal November 2015

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59 BASIC BIOLOGICAL SCIENCES
biochemistry & molecular biology
biophysics
crystallography
structural genomics
starch-utilization system
gut microbiome
metagenomics