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

Abstract

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.

Authors:
 [1];  [2];  [2];  [3];  [4];  [2];  [5];  [3];  [2];  [5];  [2];  [5];  [4];  [4];  [5];  [3];  [3];  [5];  [5];  [6] more »;  [2];  [3];  [3];  [1];  [6];  [2];  [2];  [5];  [3];  [2];  [4];  [3];  [5];  [3];  [3];  [2];  [5];  [2];  [2];  [1];  [7];  [4];  [5];  [2];  [6];  [8];  [5] « less
  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
Publication Date:
Research Org.:
SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
Sponsoring Org.:
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)
OSTI Identifier:
1625804
Grant/Contract Number:  
AC02-76SF00515; U54 GM074898
Resource Type:
Accepted Manuscript
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 66; Journal Issue: 10; Journal ID: ISSN 1744-3091
Publisher:
International Union of Crystallography
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; biochemistry & molecular biology; biophysics; crystallography; structural genomics; starch-utilization system; gut microbiome; metagenomics

Citation Formats

Bakolitsa, Constantina, Xu, Qingping, Rife, Christopher L., Abdubek, Polat, Astakhova, Tamara, Axelrod, Herbert L., Carlton, Dennis, Chen, Connie, Chiu, Hsiu-Ju, Clayton, Thomas, Das, Debanu, Deller, Marc C., Duan, Lian, Ellrott, Kyle, Farr, Carol L., Feuerhelm, Julie, Grant, Joanna C., Grzechnik, Anna, Han, Gye Won, Jaroszewski, Lukasz, Jin, Kevin K., Klock, Heath E., Knuth, Mark W., Kozbial, Piotr, Krishna, S. Sri, Kumar, Abhinav, Lam, Winnie W., Marciano, David, McMullan, Daniel, Miller, Mitchell D., Morse, Andrew T., Nigoghossian, Edward, Nopakun, Amanda, Okach, Linda, Puckett, Christina, Reyes, Ron, Tien, Henry J., Trame, Christine B., van den Bedem, Henry, Weekes, Dana, Hodgson, Keith O., Wooley, John, Elsliger, Marc-André, Deacon, Ashley M., Godzik, Adam, Lesley, Scott A., and Wilson, Ian A. Structure of BT_3984, a member of the SusD/RagB family of nutrient-binding molecules. United States: N. p., 2010. Web. doi:10.1107/s1744309110032999.
Bakolitsa, Constantina, Xu, Qingping, Rife, Christopher L., Abdubek, Polat, Astakhova, Tamara, Axelrod, Herbert L., Carlton, Dennis, Chen, Connie, Chiu, Hsiu-Ju, Clayton, Thomas, Das, Debanu, Deller, Marc C., Duan, Lian, Ellrott, Kyle, Farr, Carol L., Feuerhelm, Julie, Grant, Joanna C., Grzechnik, Anna, Han, Gye Won, Jaroszewski, Lukasz, Jin, Kevin K., Klock, Heath E., Knuth, Mark W., Kozbial, Piotr, Krishna, S. Sri, Kumar, Abhinav, Lam, Winnie W., Marciano, David, McMullan, Daniel, Miller, Mitchell D., Morse, Andrew T., Nigoghossian, Edward, Nopakun, Amanda, Okach, Linda, Puckett, Christina, Reyes, Ron, Tien, Henry J., Trame, Christine B., van den Bedem, Henry, Weekes, Dana, Hodgson, Keith O., Wooley, John, Elsliger, Marc-André, Deacon, Ashley M., Godzik, Adam, Lesley, Scott A., & Wilson, Ian A. Structure of BT_3984, a member of the SusD/RagB family of nutrient-binding molecules. United States. https://doi.org/10.1107/s1744309110032999
Bakolitsa, Constantina, Xu, Qingping, Rife, Christopher L., Abdubek, Polat, Astakhova, Tamara, Axelrod, Herbert L., Carlton, Dennis, Chen, Connie, Chiu, Hsiu-Ju, Clayton, Thomas, Das, Debanu, Deller, Marc C., Duan, Lian, Ellrott, Kyle, Farr, Carol L., Feuerhelm, Julie, Grant, Joanna C., Grzechnik, Anna, Han, Gye Won, Jaroszewski, Lukasz, Jin, Kevin K., Klock, Heath E., Knuth, Mark W., Kozbial, Piotr, Krishna, S. Sri, Kumar, Abhinav, Lam, Winnie W., Marciano, David, McMullan, Daniel, Miller, Mitchell D., Morse, Andrew T., Nigoghossian, Edward, Nopakun, Amanda, Okach, Linda, Puckett, Christina, Reyes, Ron, Tien, Henry J., Trame, Christine B., van den Bedem, Henry, Weekes, Dana, Hodgson, Keith O., Wooley, John, Elsliger, Marc-André, Deacon, Ashley M., Godzik, Adam, Lesley, Scott A., and Wilson, Ian A. Wed . "Structure of BT_3984, a member of the SusD/RagB family of nutrient-binding molecules". United States. https://doi.org/10.1107/s1744309110032999. https://www.osti.gov/servlets/purl/1625804.
@article{osti_1625804,
title = {Structure of BT_3984, a member of the SusD/RagB family of nutrient-binding molecules},
author = {Bakolitsa, Constantina and Xu, Qingping and Rife, Christopher L. and Abdubek, Polat and Astakhova, Tamara and Axelrod, Herbert L. and Carlton, Dennis and Chen, Connie and Chiu, Hsiu-Ju and Clayton, Thomas and Das, Debanu and Deller, Marc C. and Duan, Lian and Ellrott, Kyle and Farr, Carol L. and Feuerhelm, Julie and Grant, Joanna C. and Grzechnik, Anna and Han, Gye Won and Jaroszewski, Lukasz and Jin, Kevin K. and Klock, Heath E. and Knuth, Mark W. and Kozbial, Piotr and Krishna, S. Sri and Kumar, Abhinav and Lam, Winnie W. and Marciano, David and McMullan, Daniel and Miller, Mitchell D. and Morse, Andrew T. and Nigoghossian, Edward and Nopakun, Amanda and Okach, Linda and Puckett, Christina and Reyes, Ron and Tien, Henry J. and Trame, Christine B. and van den Bedem, Henry and Weekes, Dana and Hodgson, Keith O. and Wooley, John and Elsliger, Marc-André and Deacon, Ashley M. and Godzik, Adam and Lesley, Scott A. and Wilson, Ian A.},
abstractNote = {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.},
doi = {10.1107/s1744309110032999},
journal = {Acta Crystallographica. Section F},
number = 10,
volume = 66,
place = {United States},
year = {Wed Sep 22 00:00:00 EDT 2010},
month = {Wed Sep 22 00:00:00 EDT 2010}
}

Works referencing / citing this record:

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

  • Goulas, T.; Garcia-Ferrer, I.; Hutcherson, J. A.
  • Molecular Oral Microbiology, Vol. 31, Issue 6
  • DOI: 10.1111/omi.12140