Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Structural analysis of papain-like NlpC/p60 superfamily enzymes with a circularly permuted topology reveals potential lipid binding sites

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

Overview

authors

  • Xu, Q. P.
  • Rawlings, N. D.
  • Chiu, H. J.
  • Jaroszewski, L.
  • Klock, H. E.
  • Knuth, M. W.
  • Elsliger, M. A.
  • Deacon, A. M.
  • Godzik, A.
  • Lesley, Scott
  • Wilson, Ian

publication date

  • July 2011

journal

  • PLoS One  Journal

abstract

  • NlpC/P60 superfamily papain-like enzymes play important roles in all kingdoms of life. Two members of this superfamily, LRAT-like and YaeF/YiiX-like families, were predicted to contain a catalytic domain that is circularly permuted such that the catalytic cysteine is located near the C-terminus, instead of at the N-terminus. These permuted enzymes are widespread in virus, pathogenic bacteria, and eukaryotes. We determined the crystal structure of a member of the YaeF/YiiX-like family from Bacillus cereus in complex with lysine. The structure, which adopts a ligand-induced, "closed" conformation, confirms the circular permutation of catalytic residues. A comparative analysis of other related protein structures within the NlpC/P60 superfamily is presented. Permutated NlpC/P60 enzymes contain a similar conserved core and arrangement of catalytic residues, including a Cys/His-containing triad and an additional conserved tyrosine. More surprisingly, permuted enzymes have a hydrophobic S1 binding pocket that is distinct from previously characterized enzymes in the family, indicative of novel substrate specificity. Further analysis of a structural homolog, YiiX (PDB 2if6) identified a fatty acid in the conserved hydrophobic pocket, thus providing additional insights into possible function of these novel enzymes.

subject areas

  • Amino Acid Sequence
  • Bacillus cereus
  • Bacterial Proteins
  • Binding Sites
  • Biocatalysis
  • Catalytic Domain
  • Conserved Sequence
  • Fatty Acids
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Ligands
  • Lipid Metabolism
  • Lipoproteins
  • Models, Molecular
  • Molecular Sequence Data
  • Papain
scroll to property group menus

Identity

PubMed Central ID

  • PMC3142127

International Standard Serial Number (ISSN)

  • 1932-6203

Digital Object Identifier (DOI)

  • 10.1371/journal.pone.0022013

PubMed ID

  • 21799766
scroll to property group menus

Additional Document Info

start page

  • e22013

volume

  • 6

issue

  • 7

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support