• Je něco špatně v tomto záznamu ?

Structural analysis of the putative SARS-CoV-2 primase complex

E. Konkolova, M. Klima, R. Nencka, E. Boura,

. 2020 ; 211 (2) : 107548. [pub] 20200611

Jazyk angličtina Země Spojené státy americké

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc20024848

We report the crystal structure of the SARS-CoV-2 putative primase composed of the nsp7 and nsp8 proteins. We observed a dimer of dimers (2:2 nsp7-nsp8) in the crystallographic asymmetric unit. The structure revealed a fold with a helical core of the heterotetramer formed by both nsp7 and nsp8 that is flanked with two symmetry-related nsp8 β-sheet subdomains. It was also revealed that two hydrophobic interfaces one of approx. 1340 Å2 connects the nsp7 to nsp8 and a second one of approx. 950 Å2 connects the dimers and form the observed heterotetramer. Interestingly, analysis of the surface electrostatic potential revealed a putative RNA binding site that is formed only within the heterotetramer.

Citace poskytuje Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc20024848
003      
CZ-PrNML
005      
20201222154927.0
007      
ta
008      
201125s2020 xxu f 000 0|eng||
009      
AR
024    7_
$a 10.1016/j.jsb.2020.107548 $2 doi
035    __
$a (PubMed)32535228
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a xxu
100    1_
$a Konkolova, Eva $u Institute of Organic Chemistry and Biochemistry AS CR, v.v.i, Flemingovo nam. 2, 166 10 Prague 6, Czech Republic.
245    10
$a Structural analysis of the putative SARS-CoV-2 primase complex / $c E. Konkolova, M. Klima, R. Nencka, E. Boura,
520    9_
$a We report the crystal structure of the SARS-CoV-2 putative primase composed of the nsp7 and nsp8 proteins. We observed a dimer of dimers (2:2 nsp7-nsp8) in the crystallographic asymmetric unit. The structure revealed a fold with a helical core of the heterotetramer formed by both nsp7 and nsp8 that is flanked with two symmetry-related nsp8 β-sheet subdomains. It was also revealed that two hydrophobic interfaces one of approx. 1340 Å2 connects the nsp7 to nsp8 and a second one of approx. 950 Å2 connects the dimers and form the observed heterotetramer. Interestingly, analysis of the surface electrostatic potential revealed a putative RNA binding site that is formed only within the heterotetramer.
650    _2
$a Betacoronavirus $x chemie $7 D000073640
650    _2
$a vazebná místa $7 D001665
650    _2
$a krystalografie rentgenová $7 D018360
650    _2
$a DNA-primasa $x chemie $x metabolismus $7 D019915
650    _2
$a molekulární modely $7 D008958
650    _2
$a multiproteinové komplexy $7 D046912
650    _2
$a konformace proteinů $7 D011487
650    _2
$a multimerizace proteinu $7 D055503
650    _2
$a RNA $x metabolismus $7 D012313
650    _2
$a virové nestrukturální proteiny $x chemie $x metabolismus $7 D017361
655    _2
$a časopisecké články $7 D016428
655    _2
$a práce podpořená grantem $7 D013485
700    1_
$a Klima, Martin $u Institute of Organic Chemistry and Biochemistry AS CR, v.v.i, Flemingovo nam. 2, 166 10 Prague 6, Czech Republic.
700    1_
$a Nencka, Radim $u Institute of Organic Chemistry and Biochemistry AS CR, v.v.i, Flemingovo nam. 2, 166 10 Prague 6, Czech Republic.
700    1_
$a Boura, Evzen $u Institute of Organic Chemistry and Biochemistry AS CR, v.v.i, Flemingovo nam. 2, 166 10 Prague 6, Czech Republic. Electronic address: boura@uochb.cas.cz.
773    0_
$w MED00002951 $t Journal of structural biology $x 1095-8657 $g Roč. 211, č. 2 (2020), s. 107548
856    41
$u https://pubmed.ncbi.nlm.nih.gov/32535228 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y a $z 0
990    __
$a 20201125 $b ABA008
991    __
$a 20201222154923 $b ABA008
999    __
$a ok $b bmc $g 1598993 $s 1115534
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2020 $b 211 $c 2 $d 107548 $e 20200611 $i 1095-8657 $m Journal of structural biology $n J Struct Biol $x MED00002951
LZP    __
$a Pubmed-20201125

Najít záznam

Citační ukazatele

Možnosti archivace