The crystal structure of Rv2991 from Mycobacterium tuberculosis: An F420 binding protein with unknown function

被引：0

作者：

Benini, Stefano ^{[1
]}

Haouz, Ahmed ^{[2
]}

Proux, Florence ^{[2
,5
]}

Alzari, Pedro ^{[3
]}

Wilson, Keith ^{[4
]}

机构：

[1] Free Univ Bolzano, Fac Sci & Technol, Bioorgan Chem & Biocrystallog Lab B2Cl, I-39100 Bolzano, Italy

[2] Inst Pasteur, CNRS UMR 3528, Plateforme Cristallog C2RT, F-75724 Paris 15, France

[3] Univ Paris Diderot, CNRS UMR 3528, Inst Pasteur, Unite Microbiol Struct,Sorbonne Paris Cite, F-75724 Paris 15, France

[4] Univ York, Dept Chem, York Struct Biol Lab, York YO10 5DD, N Yorkshire, England

[5] Ecole Normale Super, Sect Genom Fonct, Inst Biol IBENS, 46 Rue Ulm, F-75005 Paris, France

来源：

JOURNAL OF STRUCTURAL BIOLOGY | 2019年 / 206卷 / 02期

关键词：

Structural genomics; Mycobacteriwn tuberculosis; F-420; Unknown function; FDOR; IDENTIFICATION; ALIGNMENT; BIOLOGY; GENES; TOOL;

D O I：

10.1016/j.jsb.2019.03.006

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 the conserved hypothetical protein Rv2991 from Mycobacterium tuberculosis has been solved by SAD using seleno-methionine substituted protein. The dimeric biological assembly and the sequence and fold conservation are typical of F-420 cofactor binding enzymes. Despite Rv2991 still being of unknown function, sequence and structural comparison with similar proteins enable a role to be proposed for its C terminal stretch of residues in recognizing and orienting the substrate. In addition, the C-terminus is involved in both protein folding and determining the size of the active site cavity.

引用

页码：216 / 224

页数：9

共 34 条

[1] Rv2074 is a novel F420H2-dependent biliverdin reductase in Mycobacterium tuberculosis [J].

Ahmed, F. Hafna ;

Mohamed, A. Elaaf ;

Carr, Paul D. ;

Lee, Brendon M. ;

Condic-Jurkic, Karmen ;

O'Mara, Megan L. ;

Jackson, Colin J. .

PROTEIN SCIENCE, 2016, 25 (09) :1692-1709

[2] Sequence-Structure-Function Classification of a Catalytically Diverse Oxidoreductase Superfamily in Mycobacteria [J].

Ahmed, F. Hafna ;

Carr, Paul D. ;

Lee, Brendon M. ;

Afriat-Jurnou, Livnat ;

Mohamed, A. Elaaf ;

Hong, Nan-Sook ;

Flanagan, Jack ;

Taylor, Matthew C. ;

Greening, Chris ;

Jackson, Colin J. .

JOURNAL OF MOLECULAR BIOLOGY, 2015, 427 (22) :3554-3571

[3] The 1.58 Å resolution structure of the DNA-binding domain of bacteriophage SF6 small terminase provides new hints on DNA binding [J].

Benini, Stefano ;

Chechik, Maria ;

Lombardia, Miguel Ortiz ;

Polier, Sigrun ;

Leech, Andrew ;

Shevtsov, Mikhail B. ;

Alonso, Juan C. .

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2013, 69 :376-381

[4] Generation, representation and flow of phase information in structure determination:: recent developments in and around SHARP 2.0 [J].

Bricogne, G ;

Vonrhein, C ;

Flensburg, C ;

Schiltz, M ;

Paciorek, W .

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2003, 59 :2023-2030

[5] Crystal structure of the conserved hypothetical protein Rv1155 from Mycobacterium tuberculosis [J].

Canaan, S ;

Sulzenbacher, G ;

Roig-Zamboni, V ;

Scappuccini-Calvo, L ;

Frassinetti, F ;

Maurin, D ;

Cambillau, C ;

Bourne, Y .

FEBS LETTERS, 2005, 579 (01) :215-221

[6] Metabolism of a 5-nitroimidazole in susceptible and resistant isogenic strains of Bacteroides fragilis [J].

Carlier, JP ;

Sellier, N ;

Rager, MN ;

Reysset, G .

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 1997, 41 (07) :1495-1499

[7] Structure of Ddn, the Deazaflavin-Dependent Nitroreductase from Mycobacterium tuberculosis Involved in Bioreductive Activation of PA-824 [J].

Cellitti, Susan E. ;

Shaffer, Jennifer ;

Jones, David H. ;

Mukherjee, Tathagata ;

Gurumurthy, Meera ;

Bursulaya, Badry ;

Boshoff, Helena I. ;

Choi, Inhee ;

Nayyar, Amit ;

Lee, Yong Sok ;

Cherian, Joseph ;

Niyomrattanakit, Pornwaratt ;

Dick, Thomas ;

Manjunatha, Ujjini H. ;

Barry, Clifton E., III ;

Spraggon, Glen ;

Geierstanger, Bernhard H. .

STRUCTURE, 2012, 20 (01) :101-112

[8] Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence [J].

Cole, ST ;

Brosch, R ;

Parkhill, J ;

Garnier, T ;

Churcher, C ;

Harris, D ;

Gordon, SV ;

Eiglmeier, K ;

Gas, S ;

Barry, CE ;

Tekaia, F ;

Badcock, K ;

Basham, D ;

Brown, D ;

Chillingworth, T ;

Connor, R ;

Davies, R ;

Devlin, K ;

Feltwell, T ;

Gentles, S ;

Hamlin, N ;

Holroyd, S ;

Hornby, T ;

Jagels, K ;

Krogh, A ;

McLean, J ;

Moule, S ;

Murphy, L ;

Oliver, K ;

Osborne, J ;

Quail, MA ;

Rajandream, MA ;

Rogers, J ;

Rutter, S ;

Seeger, K ;

Skelton, J ;

Squares, R ;

Squares, S ;

Sulston, JE ;

Taylor, K ;

Whitehead, S ;

Barrell, BG .

NATURE, 1998, 393 (6685) :537-+

[9] WIDESPREAD DISTRIBUTION OF A 5-DEAZAFLAVIN COFACTOR IN ACTINOMYCES AND RELATED BACTERIA [J].

DANIELS, L ;

BAKHIET, N ;

HARMON, K .

SYSTEMATIC AND APPLIED MICROBIOLOGY, 1985, 6 (01) :12-17

[10] Coot:: model-building tools for molecular graphics [J].

Emsley, P ;

Cowtan, K .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2004, 60 :2126-2132

← 1 2 3 4 →