Structure of Novel Enzyme in Mannan Biodegradation Process 4-O-β-D-Mannosyl-D-Glucose Phosphorylase MGP

被引：30

作者：

Nakae, Setsu ^{[1
,2
]}

Ito, Shigeaki ^{[3
]}

Higa, Mariko ^{[4
]}

Senoura, Takeshi ^{[5
]}

Wasaki, Jun ^{[6
]}

Hijikata, Atsushi ^{[1
,2
]}

Shionyu, Masafumi ^{[1
,2
]}

Ito, Susumu ^{[4
]}

Shirai, Tsuyoshi ^{[1
,2
]}

机构：

[1] Nagahama Inst Biosci & Technol, Dept Biosci, Nagahama 5260829, Japan

[2] Inst Bioinformat Res & Dev, Japan Sci & Technol Agcy, Nagahama 5260829, Japan

[3] Japan Tobacco Inc, Cent Tobacco Res Ctr, Yokohama, Kanagawa 2278512, Japan

[4] Univ Ryukyus, Fac Agr, Dept Biosci & Biotechnol, Nishihara, Okinawa 9030213, Japan

[5] Ishikawa Prefectural Univ, Res Inst Bioresources & Biotechnol, Nonoichi, Ishikawa 9218836, Japan

[6] Hiroshima Univ, Grad Sch Biosphere Sci, Higashihiroshima 7398521, Japan

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2013年 / 425卷 / 22期

关键词：

X-ray crystallography; biomass degradation; hemicellulose; protein evolution; CRYSTAL-STRUCTURE; ACTIVE-SITE; INSIGHTS; GENE; ROLES; EXPRESSION; COMPLEXES; MECHANISM; SYSTEM; GENOME;

D O I：

10.1016/j.jmb.2013.08.002

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The crystal structure of a novel component of the mannan biodegradation system, 4-O-beta-D-mannosyl-D-glucose phosphorylase (MGP), was determined to a 1.68-angstrom resolution. The structure of the enzyme revealed a unique homohexameric structure, which was formed by using two helices attached to the N-terminus and C-terminus as a tab for sticking between subunits. The structures of MGP complexes with genuine substrates, 4-O-beta-D-mannosyl-D-glucose and phosphate, and the product D-mannose-1-phosphate were also determined. The complex structures revealed that the invariant residue Asp131, which is supposed to be the general acid/base, did not exist close to the glycosidic Glc-O4 atom, which should be protonated in the catalytic reaction. Also, no solvent molecule that might mediate a proton transfer from Asp131 was observed in the substrate complex structure, suggesting that the catalytic mechanism of MGP is different from those of known disaccharide phosphorylases. (C) 2013 Elsevier Ltd. All rights reserved.

引用

页码：4468 / 4478

页数：11

共 39 条

[1] PHENIX: a comprehensive Python']Python-based system for macromolecular structure solution [J].

Adams, Paul D. ;

Afonine, Pavel V. ;

Bunkoczi, Gabor ;

Chen, Vincent B. ;

Davis, Ian W. ;

Echols, Nathaniel ;

Headd, Jeffrey J. ;

Hung, Li-Wei ;

Kapral, Gary J. ;

Grosse-Kunstleve, Ralf W. ;

McCoy, Airlie J. ;

Moriarty, Nigel W. ;

Oeffner, Robert ;

Read, Randy J. ;

Richardson, David C. ;

Richardson, Jane S. ;

Terwilliger, Thomas C. ;

Zwart, Peter H. .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2010, 66 :213-221

[2] iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM [J].

Battye, T. Geoff G. ;

Kontogiannis, Luke ;

Johnson, Owen ;

Powell, Harold R. ;

Leslie, Andrew G. W. .

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2011, 67 :271-281

[3] The ribosomal peptidyl transferase [J].

Beringer, Malte ;

Rodnina, Marina V. .

MOLECULAR CELL, 2007, 26 (03) :311-321

[4] The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics [J].

Cantarel, Brandi L. ;

Coutinho, Pedro M. ;

Rancurel, Corinne ;

Bernard, Thomas ;

Lombard, Vincent ;

Henrissat, Bernard .

NUCLEIC ACIDS RESEARCH, 2009, 37 :D233-D238

[5] Extensive DNA inversions in the B. fragilis genome control variable gene expression [J].

Cerdeño-Tárraga, AM ;

Patrick, S ;

Crossman, LC ;

Blakely, G ;

Abratt, V ;

Lennard, N ;

Poxton, I ;

Duerden, B ;

Harris, B ;

Quail, MA ;

Barron, A ;

Clark, L ;

Corton, C ;

Doggett, J ;

Holden, MTG ;

Larke, N ;

Line, A ;

Lord, A ;

Norbertczak, H ;

Ormond, D ;

Price, C ;

Rabbinowitsch, E ;

Woodward, J ;

Barrell, B ;

Parkhill, J .

SCIENCE, 2005, 307 (5714) :1463-1465

[6] Effect of molecular crowding on the enzymes of glycogenolysis [J].

Chebotareva, N. A. .

BIOCHEMISTRY-MOSCOW, 2007, 72 (13) :1478-1490

[7] Broadening the synthetic potential of disaccharide phosphorylases through enzyme engineering [J].

Desmet, Tom ;

Soetaert, Wim .

PROCESS BIOCHEMISTRY, 2012, 47 (01) :11-17

[8] Insights into the molecular determinants of substrate specificity in glycoside hydrolase family 5 revealed by the crystal structure and kinetics of Cellvibrio mixtus mannosidase 5A [J].

Dias, FMV ;

Vincent, F ;

Pell, G ;

Prates, JAM ;

Centeno, MSJ ;

Tailford, LE ;

Ferreira, LMA ;

Fontes, CMGA ;

Davies, GJ ;

Gilbert, HJ .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (24) :25517-25526

[9] Bacteria engineered for fuel ethanol production: current status [J].

Dien, BS ;

Cotta, MA ;

Jeffries, TW .

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 2003, 63 (03) :258-266

[10]

Ducros VMA, 2002, ANGEW CHEM INT EDIT, V41, P2824, DOI 10.1002/1521-3773(20020802)41:15<2824::AID-ANIE2824>3.0.CO

← 1 2 3 4 →