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Structure and ligand binding of the soluble domain of a Thermotoga maritima membrane protein of unknown function TM1634

Academic Article
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Overview

authors

  • McCleverty, C. J.
  • Columbus, L.
  • Kreusch, A.
  • Lesley, Scott

publication date

  • May 2008

journal

  • Protein Science  Journal

abstract

  • As a part of the Joint Center for Structural Genomics (JCSG) biological targets, the structures of soluble domains of membrane proteins from Thermotoga maritima were pursued. Here, we report the crystal structure of the soluble domain of TM1634, a putative membrane protein of 128 residues (15.1 kDa) and unknown function. The soluble domain of TM1634 is an alpha-helical dimer that contains a single tetratrico peptide repeat (TPR) motif in each monomer where each motif is similar to that found in Tom20. The overall fold, however, is unique and a DALI search does not identify similar folds beyond the 38-residue TPR motif. Two different putative ligand binding sites, in which PEG200 and Co(2+) were located, were identified using crystallography and NMR, respectively.

subject areas

  • Amino Acid Sequence
  • Bacterial Proteins
  • Binding Sites
  • Cobalt
  • Crystallography, X-Ray
  • Dimerization
  • Ligands
  • Membrane Proteins
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Polyethylene Glycols
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Sequence Deletion
  • Solubility
  • Thermotoga maritima
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Research

keywords

  • Co2+ ligand
  • PEG binding site
  • TPR motif
  • Thermotoga maritima
  • membrane protein
  • protein of unknown function
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Identity

PubMed Central ID

  • PMC2327271

International Standard Serial Number (ISSN)

  • 0961-8368

Digital Object Identifier (DOI)

  • 10.1110/ps.083432208

PubMed ID

  • 18369189
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Additional Document Info

start page

  • 869

end page

  • 877

volume

  • 17

issue

  • 5

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