Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Structure of the first representative of pfam family pf09410 (duf2006) reveals a structural signature of the calycin superfamily that suggests a role in lipid metabolism

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Chiu, H. J.
  • Bakolitsa, C.
  • Skerra, A.
  • Lomize, A.
  • Carlton, D.
  • Miller, M. D.
  • Krishna, S. S.
  • Abdubek, P.
  • Astakhova, T.
  • Axelrod, H. L.
  • Clayton, T.
  • Deller, M. C.
  • Duan, L. A.
  • Feuerhelm, J.
  • Grant, J. C.
  • Grzechnik, S. K.
  • Han, G. W.
  • Jaroszewski, L.
  • Jin, K. K.
  • Klock, H. E.
  • Knuth, M. W.
  • Kozbial, P.
  • Kumar, A.
  • Marciano, David
  • McMullan, D.
  • Morse, A. T.
  • Nigoghossian, E.
  • Okach, L.
  • Paulsen, J.
  • Reyes, R.
  • Rife, C. L.
  • van den Bedem, H.
  • Weekes, D.
  • Xu, Q. P.
  • 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 first structural representative of the domain of unknown function DUF2006 family, also known as Pfam family PF09410, comprises a lipocalin-like fold with domain duplication. The finding of the calycin signature in the N-terminal domain, combined with remote sequence similarity to two other protein families (PF07143 and PF08622) implicated in isoprenoid metabolism and the oxidative stress response, support an involvement in lipid metabolism. Clusters of conserved residues that interact with ligand mimetics suggest that the binding and regulation sites map to the N-terminal domain and to the interdomain interface, respectively.

subject areas

  • Amino Acid Sequence
  • Bacterial Proteins
  • Crystallography, X-Ray
  • Databases, Genetic
  • Lipid Metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Nitrosomonas europaea
  • Oxidative Stress
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Sequence Homology, Amino Acid
scroll to property group menus

Identity

PubMed Central ID

  • PMC2954199

International Standard Serial Number (ISSN)

  • 1744-3091

Digital Object Identifier (DOI)

  • 10.1107/s1744309109037749

PubMed ID

  • 20944205
scroll to property group menus

Additional Document Info

start page

  • 1153

end page

  • 1159

volume

  • 66

issue

  • Pt 10

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support