Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins - PubMed (original) (raw)

. 2000 Feb 3;403(6769):567-71.

doi: 10.1038/35000617.

Affiliations

• PMID: 10676968
• DOI: 10.1038/35000617

Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins

B Prakash et al. Nature. 2000.

Abstract

Interferon-gamma is an immunomodulatory substance that induces the expression of many genes to orchestrate a cellular response and establish the antiviral state of the cell. Among the most abundant antiviral proteins induced by interferon-gamma are guanylate-binding proteins such as GBP1 and GBP2. These are large GTP-binding proteins of relative molecular mass 67,000 with a high-turnover GTPase activity and an antiviral effect. Here we have determined the crystal structure of full-length human GBP1 to 1.8 A resolution. The amino-terminal 278 residues constitute a modified G domain with a number of insertions compared to the canonical Ras structure, and the carboxy-terminal part is an extended helical domain with unique features. From the structure and biochemical experiments reported here, GBP1 appears to belong to the group of large GTP-binding proteins that includes Mx and dynamin, the common property of which is the ability to undergo oligomerization with a high concentration-dependent GTPase activity.

PubMed Disclaimer

Similar articles

• How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP.
  Ghosh A, Praefcke GJ, Renault L, Wittinghofer A, Herrmann C. Ghosh A, et al. Nature. 2006 Mar 2;440(7080):101-4. doi: 10.1038/nature04510. Nature. 2006. PMID: 16511497
• Structure of Cdc42 in complex with the GTPase-binding domain of the 'Wiskott-Aldrich syndrome' protein.
  Abdul-Manan N, Aghazadeh B, Liu GA, Majumdar A, Ouerfelli O, Siminovitch KA, Rosen MK. Abdul-Manan N, et al. Nature. 1999 May 27;399(6734):379-83. doi: 10.1038/20726. Nature. 1999. PMID: 10360578
• Identification of residues in the human guanylate-binding protein 1 critical for nucleotide binding and cooperative GTP hydrolysis.
  Praefcke GJ, Kloep S, Benscheid U, Lilie H, Prakash B, Herrmann C. Praefcke GJ, et al. J Mol Biol. 2004 Nov 12;344(1):257-69. doi: 10.1016/j.jmb.2004.09.026. J Mol Biol. 2004. PMID: 15504415
• Structure of small G proteins and their regulators.
  Paduch M, Jeleń F, Otlewski J. Paduch M, et al. Acta Biochim Pol. 2001;48(4):829-50. Acta Biochim Pol. 2001. PMID: 11995995 Review.
• The dynamin superfamily: universal membrane tubulation and fission molecules?
  Praefcke GJ, McMahon HT. Praefcke GJ, et al. Nat Rev Mol Cell Biol. 2004 Feb;5(2):133-47. doi: 10.1038/nrm1313. Nat Rev Mol Cell Biol. 2004. PMID: 15040446 Review.

Cited by

• Invited review: Mechanisms of GTP hydrolysis and conformational transitions in the dynamin superfamily.
  Daumke O, Praefcke GJ. Daumke O, et al. Biopolymers. 2016 Aug;105(8):580-93. doi: 10.1002/bip.22855. Biopolymers. 2016. PMID: 27062152 Free PMC article. Review.
• Structural basis for GTP-induced dimerization and antiviral function of guanylate-binding proteins.
  Cui W, Braun E, Wang W, Tang J, Zheng Y, Slater B, Li N, Chen C, Liu Q, Wang B, Li X, Duan Y, Xiao Y, Ti R, Hotter D, Ji X, Zhang L, Cui J, Xiong Y, Sauter D, Wang Z, Kirchhoff F, Yang H. Cui W, et al. Proc Natl Acad Sci U S A. 2021 Apr 13;118(15):e2022269118. doi: 10.1073/pnas.2022269118. Proc Natl Acad Sci U S A. 2021. PMID: 33876762 Free PMC article.
• Dynamin-like MxA GTPase: structural insights into oligomerization and implications for antiviral activity.
  Haller O, Gao S, von der Malsburg A, Daumke O, Kochs G. Haller O, et al. J Biol Chem. 2010 Sep 10;285(37):28419-24. doi: 10.1074/jbc.R110.145839. Epub 2010 Jun 10. J Biol Chem. 2010. PMID: 20538602 Free PMC article. Review.
• Role of Clathrin and Dynamin in Clathrin Mediated Endocytosis/Synaptic Vesicle Recycling and Implications in Neurological Diseases.
  Prichard KL, O'Brien NS, Murcia SR, Baker JR, McCluskey A. Prichard KL, et al. Front Cell Neurosci. 2022 Jan 18;15:754110. doi: 10.3389/fncel.2021.754110. eCollection 2021. Front Cell Neurosci. 2022. PMID: 35115907 Free PMC article. Review.
• The helical domain of GBP-1 mediates the inhibition of endothelial cell proliferation by inflammatory cytokines.
  Guenzi E, Töpolt K, Cornali E, Lubeseder-Martellato C, Jörg A, Matzen K, Zietz C, Kremmer E, Nappi F, Schwemmle M, Hohenadl C, Barillari G, Tschachler E, Monini P, Ensoli B, Stürzl M. Guenzi E, et al. EMBO J. 2001 Oct 15;20(20):5568-77. doi: 10.1093/emboj/20.20.5568. EMBO J. 2001. PMID: 11598000 Free PMC article.

Publication types

MeSH terms

Substances

LinkOut - more resources

• Full Text Sources

  • Nature Publishing Group
  • Ovid Technologies, Inc.

• Other Literature Sources

  • The Lens - Patent Citations Database

• Molecular Biology Databases

  • BioCyc
  • Gene Ontology
  • GlyGen glycoinformatics resource
  • Saccharomyces Genome Database

• Research Materials

  • NCI CPTC Antibody Characterization Program