دورية أكاديمية

Structure of the Arabidopsis Glutamate Receptor-like Channel GLR3.2 Ligand-Binding Domain.

التفاصيل البيبلوغرافية
العنوان: Structure of the Arabidopsis Glutamate Receptor-like Channel GLR3.2 Ligand-Binding Domain.
المؤلفون: Gangwar SP; Department of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168(th) Street, New York, NY 10032, USA., Green MN; Department of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168(th) Street, New York, NY 10032, USA; Training Program in Nutritional and Metabolic Biology, Institute of Human Nutrition, Columbia University Irving Medical Center, 630 West 168(th) Street, New York, NY 10032, USA., Michard E; Department of Cell Biology and Molecular Genetics, University of Maryland, 0118 BioScience Research Bldg, College Park, MD 20742-5815, USA., Simon AA; Department of Cell Biology and Molecular Genetics, University of Maryland, 0118 BioScience Research Bldg, College Park, MD 20742-5815, USA., Feijó JA; Department of Cell Biology and Molecular Genetics, University of Maryland, 0118 BioScience Research Bldg, College Park, MD 20742-5815, USA. Electronic address: jfeijo@umd.edu., Sobolevsky AI; Department of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168(th) Street, New York, NY 10032, USA. Electronic address: as4005@cumc.columbia.edu.
المصدر: Structure (London, England : 1993) [Structure] 2021 Feb 04; Vol. 29 (2), pp. 161-169.e4. Date of Electronic Publication: 2020 Oct 06.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
اللغة: English
بيانات الدورية: Publisher: Cell Press Country of Publication: United States NLM ID: 101087697 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1878-4186 (Electronic) Linking ISSN: 09692126 NLM ISO Abbreviation: Structure Subsets: MEDLINE
أسماء مطبوعة: Publication: 2000- : Cambridge, Mass. : Cell Press
Original Publication: London : Current Biology, c1993-
مواضيع طبية MeSH: Arabidopsis Proteins/*chemistry , Receptors, Glutamate/*chemistry, Arabidopsis ; Arabidopsis Proteins/agonists ; Arabidopsis Proteins/metabolism ; Binding Sites ; Ion Channel Gating ; Molecular Dynamics Simulation ; Protein Binding ; Receptors, Glutamate/metabolism
مستخلص: Glutamate receptor-like channels (GLRs) play important roles in numerous plant physiological processes. GLRs are homologous to ionotropic glutamate receptors (iGluRs) that mediate neurotransmission in vertebrates. Here we determine crystal structures of Arabidopsis thaliana GLR3.2 ligand-binding domain (LBD) in complex with glycine and methionine to 1.58- and 1.75-Å resolution, respectively. Our structures show a fold similar to that of iGluRs, but with several secondary structure elements either missing or different. The closed clamshell conformation of GLR3.2 LBD suggests that both glycine and methionine act as agonists. The mutation R133A strongly increases the constitutive activity of the channel, suggesting that the LBD mutated at the residue critical for agonist binding produces a more stable closed clamshell conformation. Furthermore, our structures explain the promiscuity of GLR activation by different amino acids, confirm evolutionary conservation of structure between GLRs and iGluRs, and predict common molecular principles of their gating mechanisms driven by bilobed clamshell-like LBDs.
Competing Interests: Declaration of Interests The authors declare no competing interests.
(Copyright © 2020 Elsevier Ltd. All rights reserved.)
References: J Neurosci. 2012 Jul 18;32(29):9796-804. (PMID: 22815494)
J Mol Biol. 2001 Aug 24;311(4):815-36. (PMID: 11518533)
J Physiol. 2015 Jan 1;593(1):29-38. (PMID: 25556785)
Cell Rep. 2016 Dec 6;17(10):2553-2561. (PMID: 27926860)
J Physiol. 2020 Jan 25;:. (PMID: 31981421)
Protein Eng. 1995 Feb;8(2):127-34. (PMID: 7630882)
Protein Sci. 2018 Jan;27(1):129-134. (PMID: 28875543)
Nat Commun. 2020 Aug 14;11(1):4082. (PMID: 32796832)
J Exp Bot. 2016 Mar;67(6):1853-69. (PMID: 26773810)
J Neurosci. 2011 May 4;31(18):6928-38. (PMID: 21543622)
Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):235-42. (PMID: 21460441)
Structure. 2013 Mar 5;21(3):414-25. (PMID: 23434404)
Trends Neurosci. 2004 Jun;27(6):321-8. (PMID: 15165736)
Nat Commun. 2017 Feb 17;8:14327. (PMID: 28211453)
Sci Signal. 2013 Jun 11;6(279):ra47. (PMID: 23757024)
Nature. 2014 Oct 16;514(7522):328-34. (PMID: 25119039)
J Biol Chem. 2008 Aug 1;283(31):21519-29. (PMID: 18450751)
Neuropharmacology. 2011 Jan;60(1):135-50. (PMID: 20713069)
Neuron. 2000 Oct;28(1):165-81. (PMID: 11086992)
J Physiol. 2004 Jan 15;554(Pt 2):249-53. (PMID: 14645452)
Annu Rev Physiol. 2013;75:313-37. (PMID: 22974439)
F1000Prime Rep. 2014 Jun 02;6:37. (PMID: 24991414)
Neuron. 2010 Dec 22;68(6):1082-96. (PMID: 21172611)
Nature. 1998 Nov 12;396(6707):125-6. (PMID: 9823891)
Science. 2001 May 25;292(5521):1486-7. (PMID: 11379626)
J Mol Biol. 2008 Feb 15;376(2):308-16. (PMID: 18164033)
Nature. 1998 Oct 29;395(6705):913-7. (PMID: 9804426)
Pharmacol Rev. 2010 Sep;62(3):405-96. (PMID: 20716669)
Plant Cell Physiol. 2001 Jan;42(1):74-84. (PMID: 11158446)
Neuron. 2005 Feb 17;45(4):539-52. (PMID: 15721240)
Plant Physiol. 2015 Apr;167(4):1630-42. (PMID: 25681329)
Nat Neurosci. 2003 Aug;6(8):803-10. (PMID: 12872125)
Neuropharmacology. 2017 Jan;112(Pt A):16-28. (PMID: 27236079)
Plant Physiol. 2013 Jul;162(3):1497-509. (PMID: 23656893)
J Biol Chem. 2012 Dec 21;287(52):43557-64. (PMID: 23115239)
Nature. 2017 Sep 7;549(7670):91-95. (PMID: 28737761)
EMBO J. 2003 Jun 16;22(12):2873-85. (PMID: 12805203)
Front Plant Sci. 2012 Oct 30;3:235. (PMID: 23115559)
Nature. 2005 Nov 10;438(7065):185-92. (PMID: 16281028)
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32. (PMID: 15572765)
Science. 2018 May 4;360(6388):533-536. (PMID: 29724955)
Biophys Chem. 2016 Nov;218:14-26. (PMID: 27586818)
Science. 2009 Mar 6;323(5919):1313-9. (PMID: 19265014)
Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):213-21. (PMID: 20124702)
Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):125-32. (PMID: 20124692)
Acta Crystallogr D Biol Crystallogr. 2007 Jan;63(Pt 1):32-41. (PMID: 17164524)
Biochemistry. 2018 Jan 23;57(3):267-276. (PMID: 29037031)
Nucleic Acids Res. 2018 Jul 2;46(W1):W296-W303. (PMID: 29788355)
Proc Natl Acad Sci U S A. 2010 Sep 14;107(37):16315-9. (PMID: 20805473)
Mol Biol Evol. 2002 Jul;19(7):1066-82. (PMID: 12082126)
Proc Natl Acad Sci U S A. 2003 May 13;100(10):5736-41. (PMID: 12730367)
Plant Physiol. 2012 May;159(1):40-6. (PMID: 22447719)
Proc Natl Acad Sci U S A. 2020 Jan 7;117(1):752-760. (PMID: 31871183)
Science. 2011 Apr 22;332(6028):434-7. (PMID: 21415319)
Nature. 2009 Dec 10;462(7274):745-56. (PMID: 19946266)
Nat Methods. 2009 May;6(5):343-5. (PMID: 19363495)
Nature. 2013 Aug 22;500(7463):422-6. (PMID: 23969459)
Plant Cell. 2013 Apr;25(4):1304-13. (PMID: 23590882)
Cell. 2018 Nov 29;175(6):1520-1532.e15. (PMID: 30500536)
J Exp Bot. 2018 Apr 19;:. (PMID: 29684179)
Gene. 2012 Feb 1;493(1):36-43. (PMID: 22143033)
معلومات مُعتمدة: T32 DK007647 United States DK NIDDK NIH HHS; R01 NS107253 United States NS NINDS NIH HHS; P30 GM124165 United States GM NIGMS NIH HHS; R01 NS083660 United States NS NINDS NIH HHS; R01 CA206573 United States CA NCI NIH HHS; S10 RR029205 United States RR NCRR NIH HHS; R01 GM131043 United States GM NIGMS NIH HHS
فهرسة مساهمة: Keywords: Ca(2+) channels; X-ray crystallography; glutamate receptor-like channels (GLR); ionotropic glutamate receptor (iGluR); plant
المشرفين على المادة: 0 (Arabidopsis Proteins)
0 (GLR3.2 protein, Arabidopsis)
0 (Receptors, Glutamate)
تواريخ الأحداث: Date Created: 20201007 Date Completed: 20211123 Latest Revision: 20211123
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC7867599
DOI: 10.1016/j.str.2020.09.006
PMID: 33027636
قاعدة البيانات: MEDLINE
الوصف
تدمد:1878-4186
DOI:10.1016/j.str.2020.09.006