Structural basis of keto acid utilization in nonribosomal depsipeptide synthesis

被引：31

作者：

Alonzo, Diego A. ^{[1
,2
]}

Chiche-Lapierre, Clarisse ^{[1
,2
]}

Tarry, Michael J. ^{[1
,2
]}

Wang, Jimin ^{[3
]}

Schmeing, T. Martin ^{[1
,2
]}

机构：

[1] McGill Univ, Dept Biochem, Montreal, PQ, Canada

[2] McGill Univ, Ctr Rech Biol Struct, Montreal, PQ, Canada

[3] Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT USA

来源：

NATURE CHEMICAL BIOLOGY | 2020年 / 16卷 / 05期

基金：

加拿大自然科学与工程研究理事会;

关键词：

CARBONYL-CARBONYL INTERACTIONS; BIOSYNTHETIC GENE-CLUSTER; ANTICANCER AGENTS; ADENYLATION; VALINOMYCIN; ACTIVATION; FEATURES; DOMAINS; CLONING; MODULE;

D O I：

10.1038/s41589-020-0481-5

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：

Nonribosomal depsipeptides are natural products composed of amino and hydroxy acid residues. The hydroxy acid residues often derive from alpha-keto acids, reduced by ketoreductase domains in the depsipeptide synthetases. Biochemistry and structures reveal the mechanism of discrimination for alpha-keto acids and a remarkable architecture: flanking intact adenylation and ketoreductase domains are sequences separated by >1,100 residues that form a split 'pseudoA(sub)' domain, structurally important for the depsipeptide module's synthetic cycle.

引用

页码：493 / +

页数：9

共 44 条

[1] Advances, Interactions, and Future Developments in the CNS, Phenix, and Rosetta Structural Biology Software Systems [J].

Adams, Paul D. ;

Baker, David ;

Brunger, Axel T. ;

Das, Rhiju ;

DiMaio, Frank ;

Read, Randy J. ;

Richardson, David C. ;

Richardson, Jane S. ;

Terwilliger, Thomas C. .

ANNUAL REVIEW OF BIOPHYSICS, VOL 42, 2013, 42 :265-287

[2] Carbonyl-carbonyl interactions can be competitive with hydrogen bonds [J].

Allen, FH ;

Baalham, CA ;

Lommerse, JPM ;

Raithby, PR .

ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE, 1998, 54 :320-329

[3] Characterization of Cereulide Synthetase, a Toxin-Producing Macromolecular Machine [J].

Alonzo, Diego A. ;

Magarvey, Nathan A. ;

Schmeing, T. Martin .

PLOS ONE, 2015, 10 (06)

[4] 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

[5] SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information [J].

Biasini, Marco ;

Bienert, Stefan ;

Waterhouse, Andrew ;

Arnold, Konstantin ;

Studer, Gabriel ;

Schmidt, Tobias ;

Kiefer, Florian ;

Cassarino, Tiziano Gallo ;

Bertoni, Martino ;

Bordoli, Lorenza ;

Schwede, Torsten .

NUCLEIC ACIDS RESEARCH, 2014, 42 (W1) :W252-W258

[6] Predictive, structure-based model of amino acid recognition by nonribosomal peptide synthetase adenylation domains [J].

Challis, GL ;

Ravel, J ;

Townsend, CA .

CHEMISTRY & BIOLOGY, 2000, 7 (03) :211-224

[7] The nonredundant roles of two 4′-phosphopantetheinyl transferases in vital processes of Mycobacteria [J].

Chalut, C ;

Botella, L ;

de Sousa-D'Auria, C ;

Houssin, C ;

Guilhot, C .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (22) :8511-8516

[8] Deciphering the biosynthetic codes for the potent anti-SARS-CoV cyclodepsipeptide valinomycin in Streptomyces tsusimaensis ATCC 15141 [J].

Cheng, YQ .

CHEMBIOCHEM, 2006, 7 (03) :471-477

[9] Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S [J].

Conti, E ;

Stachelhaus, T ;

Marahiel, MA ;

Brick, P .

EMBO JOURNAL, 1997, 16 (14) :4174-4183

[10] Microseed matrix screening for optimization in protein crystallization: what have we learned? [J].

D'Arcy, Allan ;

Bergfors, Terese ;

Cowan-Jacob, Sandra W. ;

Marsh, May .

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2014, 70 :1117-1126

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