دورية أكاديمية
أعرض في EDS

Exploring the Molecular Basis for Substrate Affinity and Structural Stability in Bacterial GH39 β-Xylosidases.

التفاصيل البيبلوغرافية
العنوان: Exploring the Molecular Basis for Substrate Affinity and Structural Stability in Bacterial GH39 β-Xylosidases.
المؤلفون: de Morais MAB; Brazilian Biorenewables National Laboratory, Brazilian Center for Research in Energy and Materials, Campinas, Brazil., Polo CC; Brazilian Synchrotron Light Laboratory, Brazilian Center for Research in Energy and Materials, Campinas, Brazil., Domingues MN; Brazilian Biorenewables National Laboratory, Brazilian Center for Research in Energy and Materials, Campinas, Brazil., Persinoti GF; Brazilian Biorenewables National Laboratory, Brazilian Center for Research in Energy and Materials, Campinas, Brazil., Pirolla RAS; Brazilian Biorenewables National Laboratory, Brazilian Center for Research in Energy and Materials, Campinas, Brazil., de Souza FHM; Brazilian Biorenewables National Laboratory, Brazilian Center for Research in Energy and Materials, Campinas, Brazil., Correa JBL; Brazilian Biorenewables National Laboratory, Brazilian Center for Research in Energy and Materials, Campinas, Brazil., Dos Santos CR; Brazilian Biorenewables National Laboratory, Brazilian Center for Research in Energy and Materials, Campinas, Brazil., Murakami MT; Brazilian Biorenewables National Laboratory, Brazilian Center for Research in Energy and Materials, Campinas, Brazil.
المصدر: Frontiers in bioengineering and biotechnology [Front Bioeng Biotechnol] 2020 May 15; Vol. 8, pp. 419. Date of Electronic Publication: 2020 May 15 (Print Publication: 2020).
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Frontiers Media S.A Country of Publication: Switzerland NLM ID: 101632513 Publication Model: eCollection Cited Medium: Print ISSN: 2296-4185 (Print) Linking ISSN: 22964185 NLM ISO Abbreviation: Front Bioeng Biotechnol Subsets: PubMed not MEDLINE
أسماء مطبوعة: Original Publication: Lausanne : Frontiers Media S.A., [2013]-
مستخلص: The glycoside hydrolase family 39 (GH39) is a functionally expanding family with limited understanding about the molecular basis for substrate specificity and extremophilicity. In this work, we demonstrate the key role of the positive-subsite region in modulating substrate affinity and how the lack of a C-terminal extension impacts on oligomerization and structural stability of some GH39 members. The crystallographic and SAXS structures of a new GH39 member from the phytopathogen Xanthomonas citri support the importance of an extended C-terminal to promote oligomerization as a molecular strategy to enhance thermal stability. Comparative structural analysis along with site-directed mutagenesis showed that two residues located at the positive-subsite region, Lys166 and Asp167, are critical to substrate affinity and catalytic performance, by inducing local changes in the active site for substrate binding. These findings expand the molecular understanding of the mechanisms involved in substrate recognition and structural stability of the GH39 family, which might be instrumental for biological insights, rational enzyme engineering and utilization in biorefineries.
(Copyright © 2020 Morais, Polo, Domingues, Persinoti, Pirolla, de Souza, Correa, dos Santos and Murakami.)
References: Science. 2012 May 25;336(6084):1030-3. (PMID: 22628654)
Sci Rep. 2016 Mar 31;6:23776. (PMID: 27029646)
J Chem Theory Comput. 2015 Aug 11;11(8):3696-713. (PMID: 26574453)
Acta Crystallogr D Biol Crystallogr. 2012 Oct;68(Pt 10):1339-45. (PMID: 22993088)
J Struct Biol. 2017 Mar;197(3):227-235. (PMID: 27890857)
J Synchrotron Radiat. 1997 Mar 1;4(Pt 2):67-77. (PMID: 16699210)
J Mol Biol. 2005 Nov 4;353(4):838-46. (PMID: 16212978)
J Biol Chem. 2018 Aug 31;293(35):13636-13649. (PMID: 29997257)
PLoS One. 2014 Aug 15;9(8):e105264. (PMID: 25127169)
Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):125-32. (PMID: 20124692)
Appl Biochem Biotechnol. 2012 Dec;168(8):2218-29. (PMID: 23054825)
New Phytol. 2013 May;198(3):899-915. (PMID: 23442088)
J Biol Chem. 2014 Nov 14;289(46):32186-32200. (PMID: 25266726)
Nucleic Acids Res. 2002 Jul 15;30(14):3059-66. (PMID: 12136088)
J Mol Graph. 1996 Feb;14(1):33-8, 27-8. (PMID: 8744570)
Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):12-21. (PMID: 20057044)
Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):240-55. (PMID: 15299926)
Biophys J. 1999 Jun;76(6):2879-86. (PMID: 10354416)
J Biol Chem. 2016 Mar 25;291(13):7183-94. (PMID: 26755730)
Biochem J. 1998 Oct 15;335 ( Pt 2):449-55. (PMID: 9761746)
J Mol Biol. 2004 Jan 2;335(1):155-65. (PMID: 14659747)
J Mol Biol. 2007 Sep 21;372(3):774-97. (PMID: 17681537)
J Biol Chem. 2015 Nov 20;290(47):28374-28387. (PMID: 26424791)
FEBS Lett. 2001 Apr 20;495(1-2):115-9. (PMID: 11322958)
Biochemistry. 2002 Aug 6;41(31):9727-35. (PMID: 12146938)
Acta Crystallogr D Biol Crystallogr. 2012 Apr;68(Pt 4):352-67. (PMID: 22505256)
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32. (PMID: 15572765)
J Biol Chem. 2013 Apr 5;288(14):9755-9766. (PMID: 23430743)
PLoS One. 2010 Mar 10;5(3):e9490. (PMID: 20224823)
Nature. 2002 May 23;417(6887):459-63. (PMID: 12024217)
Bioresour Technol. 2010 Dec;101(24):9624-30. (PMID: 20708404)
J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674. (PMID: 19461840)
J Appl Crystallogr. 2009 Apr 1;42(Pt 2):342-346. (PMID: 27630371)
J Biol Chem. 2017 Jul 28;292(30):12606-12620. (PMID: 28588026)
New Phytol. 2010 Sep;187(4):983-1002. (PMID: 20524995)
Proteins. 2005 Dec 1;61(4):704-21. (PMID: 16231289)
Mol Plant Microbe Interact. 2005 Aug;18(8):830-7. (PMID: 16134895)
Nucleic Acids Res. 2014 Jan;42(Database issue):D490-5. (PMID: 24270786)
فهرسة مساهمة: Keywords: X-ray crystallography; Xanthomonas citri; glycoside hydrolase family 39; structural stability; substrate specificity
تواريخ الأحداث: Date Created: 20200606 Latest Revision: 20240328
رمز التحديث: 20240329
مُعرف محوري في PubMed: PMC7242879
DOI: 10.3389/fbioe.2020.00419
PMID: 32500063
قاعدة البيانات: MEDLINE
الوصف
تدمد:2296-4185
DOI:10.3389/fbioe.2020.00419