Metal binding properties of Escherichia coli YjiA, a member of the metal homeostasis-associated COG0523 family of GTPases.

Item request has been placed! ×
Item request cannot be made. ×
loading   Processing Request
Read More Add to Saved list
  • Additional Information
    • Source:
      Publisher: American Chemical Society Country of Publication: United States NLM ID: 0370623 Publication Model: Print Cited Medium: Internet ISSN: 1520-4995 (Electronic) Linking ISSN: 00062960 NLM ISO Abbreviation: Biochemistry Subsets: MEDLINE
    • Publication Information:
      Original Publication: Washington, American Chemical Society.
    • Subject Terms:
      Escherichia coli/*enzymology ; Escherichia coli Proteins/*chemistry ; Escherichia coli Proteins/*metabolism ; GTP Phosphohydrolases/*chemistry ; GTP Phosphohydrolases/*metabolism; Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites/genetics ; Crystallography, X-Ray ; Escherichia coli/genetics ; Escherichia coli Proteins/genetics ; GTP Phosphohydrolases/genetics ; Kinetics ; Metals/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutant Proteins/chemistry ; Mutant Proteins/genetics ; Mutant Proteins/metabolism ; Protein Structure, Tertiary ; Sequence Homology, Amino Acid ; Zinc/metabolism
    • Abstract:
      GTPases are critical molecular switches involved in a wide range of biological functions. Recent phylogenetic and genomic analyses of the large, mostly uncharacterized COG0523 subfamily of GTPases revealed a link between some COG0523 proteins and metal homeostasis pathways. In this report, we detail the bioinorganic characterization of YjiA, a representative member of COG0523 subgroup 9 and the only COG0523 protein to date with high-resolution structural information. We find that YjiA is capable of binding several types of transition metals with dissociation constants in the low micromolar range and that metal binding affects both the oligomeric structure and GTPase activity of the enzyme. Using a combination of X-ray crystallography and site-directed mutagenesis, we identify, among others, a metal-binding site adjacent to the nucleotide-binding site in the GTPase domain that involves a conserved cysteine and several glutamate residues. Mutations of the coordinating residues decrease the impact of metal, suggesting that metal binding to this site is responsible for modulating the GTPase activity of the protein. These findings point toward a regulatory function for these COG0523 GTPases that is responsive to their metal-bound state.
    • Comments:
      Erratum in: Biochemistry. 2013 Jun 11;52(23):4105.
    • References:
      Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):235-42. (PMID: 21460441)
      J Bacteriol. 1998 Nov;180(22):5815-21. (PMID: 9811636)
      Bioinformatics. 2008 Dec 1;24(23):2780-1. (PMID: 18818215)
      Anal Biochem. 1985 Apr;146(1):150-7. (PMID: 3887984)
      J Mol Biol. 2007 Sep 21;372(3):774-97. (PMID: 17681537)
      Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501. (PMID: 20383002)
      Nat Prod Rep. 2010 May;27(5):681-94. (PMID: 20442959)
      RNA Biol. 2010 Sep-Oct;7(5):521-7. (PMID: 20657179)
      Acta Crystallogr D Biol Crystallogr. 2006 Apr;62(Pt 4):439-50. (PMID: 16552146)
      Front Microbiol. 2012 Apr 11;3:142. (PMID: 22514551)
      Inorg Chem. 2005 Nov 14;44(23):8234-42. (PMID: 16270960)
      BMC Genomics. 2009 Oct 12;10:470. (PMID: 19822009)
      J Mol Biol. 2002 Mar 15;317(1):41-72. (PMID: 11916378)
      Proteins. 2009 Jan;74(1):222-39. (PMID: 18767150)
      FEBS Lett. 2003 Oct 23;553(3):391-6. (PMID: 14572657)
      Chem Rev. 2007 Oct;107(10):4206-72. (PMID: 17927159)
      Physiol Rev. 2001 Jan;81(1):153-208. (PMID: 11152757)
      Mol Cell. 2011 Feb 4;41(3):286-97. (PMID: 21292161)
      Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):12-21. (PMID: 20057044)
      J Biol Chem. 2012 Feb 24;287(9):6753-63. (PMID: 22179820)
      Acc Chem Res. 2011 Jul 19;44(7):520-30. (PMID: 21542631)
      Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):905-21. (PMID: 9757107)
      Acta Crystallogr D Biol Crystallogr. 2008 Jan;64(Pt 1):61-9. (PMID: 18094468)
      Nature. 1990 Nov 8;348(6297):125-32. (PMID: 2122258)
      Trends Biochem Sci. 1990 Nov;15(11):430-4. (PMID: 2126155)
      Methods Enzymol. 1997;276:307-26. (PMID: 27754618)
      Chem Rev. 2009 Oct;109(10):4617-43. (PMID: 19711977)
      Proteins. 2012 Feb;80(2):374-81. (PMID: 22095872)
      Biochemistry. 2011 Dec 20;50(50):10761-3. (PMID: 22085337)
      Proteins. 2004 Feb 1;54(2):371-4. (PMID: 14696199)
      Proteins. 2007 Nov 15;69(3):466-75. (PMID: 17623850)
      J Neurochem. 2008 Mar;104(5):1249-59. (PMID: 18289347)
      Inorg Chem. 2009 Aug 3;48(15):7280-93. (PMID: 19572492)
      Anal Biochem. 1979 Nov 15;100(1):95-7. (PMID: 161695)
      Nucleic Acids Res. 2010 Jan;38(Database issue):D111-8. (PMID: 19884135)
      Mol Microbiol. 2002 Apr;44(1):89-105. (PMID: 11967071)
      Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):213-21. (PMID: 20124702)
      Biochem Soc Trans. 2005 Aug;33(Pt 4):815-9. (PMID: 16042605)
      J Bacteriol. 2012 May;194(10):2426-36. (PMID: 22389488)
      Biometals. 2007 Jun;20(3-4):485-99. (PMID: 17216355)
      J Bacteriol. 1991 Oct;173(19):6074-87. (PMID: 1655697)
      Bioinformatics. 2007 May 1;23(9):1073-9. (PMID: 17332019)
      J Biol Chem. 2006 Sep 15;281(37):27492-502. (PMID: 16807243)
      Metallomics. 2012 May;4(5):488-97. (PMID: 22511334)
      Microbiol Mol Biol Rev. 2011 Sep;75(3):507-42, second and third pages of table of contents. (PMID: 21885683)
      J Bacteriol. 2011 Mar;193(6):1359-68. (PMID: 21239585)
      J Biol Inorg Chem. 2011 Aug;16(6):857-68. (PMID: 21544686)
      Anal Biochem. 2004 Dec 1;335(1):103-11. (PMID: 15519577)
      J Biol Chem. 2003 Oct 17;278(42):41148-59. (PMID: 12869542)
      Biochemistry. 1978 Aug 8;17(16):3333-8. (PMID: 687587)
      Biochim Biophys Acta. 2005 Aug 10;1751(2):119-39. (PMID: 16027053)
      BMC Genomics. 2010 Jan 07;11:12. (PMID: 20055984)
      J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674. (PMID: 19461840)
      J Bacteriol. 1993 Feb;175(3):630-5. (PMID: 8423137)
      Anal Biochem. 1989 Nov 1;182(2):319-26. (PMID: 2610349)
      Nat Methods. 2006 Aug;3(8):623-8. (PMID: 16862137)
    • Grant Information:
      R01 GM069857 United States GM NIGMS NIH HHS; P41RR001209 United States RR NCRR NIH HHS; P41 RR001209 United States RR NCRR NIH HHS; P41GM103393 United States GM NIGMS NIH HHS; P41 GM103393 United States GM NIGMS NIH HHS
    • Accession Number:
      0 (Escherichia coli Proteins)
      0 (Metals)
      0 (Mutant Proteins)
      EC 3.6.1.- (GTP Phosphohydrolases)
      EC 3.6.1.- (YjiA protein, E coli)
      J41CSQ7QDS (Zinc)
    • Publication Date:
      Date Created: 20140123 Date Completed: 20140131 Latest Revision: 20230106
    • Publication Date:
      20230106
    • Accession Number:
      PMC3596956
    • Accession Number:
      10.1021/bi301600z
    • Accession Number:
      24449932