SARS-CoV-2 protein NSP7
From Proteopedia
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| - | <SX viewer='molstar' load='' size='340' side='right' caption='' scene=''> | + | <SX viewer='molstar' load='6yhu' size='340' side='right' caption=' Crystal structure of the nsp7-nsp8 complex of SARS-CoV-2.' scene=''> |
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'''Non-structural protein 7 (nsp7)''' | '''Non-structural protein 7 (nsp7)''' | ||
| - | Forms a hexadecamer with [[SARS-CoV-2_protein_NSP8|nsp8]] (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.<ref>[https://zhanglab.ccmb.med.umich.edu/COVID-19/ Modeling of the SARS-COV-2 Genome]</ref><ref>pmid 32200634</ref> | ||
| - | == | + | ==Function== |
| + | Nsp7 and two different conformations of [[SARS-CoV-2_protein_NSP8|nsp8]] work as a co-factor for [[SARS-CoV-2 enzyme RdRp|nsp12]]. Together they form the minimal core polymerase complex, as without its co-factors, nsp12 has a low efficiency in polymerase activity. This complex mediates the RNA synthesis of the virus and is therefore an important part in the replication process <ref name="Peng"> PMID: 32531208</ref>. It is suggested that the nsp7-nsp8 dimer might act as a primase in the complex<ref name="Konkolova"> PMID: 32535228</ref>. | ||
| - | == | + | ==Disease== |
| + | The global COVID-19 pandemic, which started in 2019, is caused by the SARS-CoV-2. | ||
| - | == | + | ==Structure== |
| + | The nsp7 is encoded on the open reading frame ORF1a and comprises 83 amino acids<ref name="Konkolova"/>. It forms a heterodimer with nsp8 to bind to nsp12 above the thumb domain of the RNA-dependent RNA polymerase (RdRp), mostly mediated by the nsp7. With this interaction, the conformation of the finger extension loops of the nsp12 are stabilized<ref name="Peng"/>. | ||
| + | Nsp7 adopts a three helical bundle fold (α1: K2-L20, α2: S26-L41 and α3: T45-S61) <ref name="Konkolova"/>. α1 and α3 interact with the α1 and α2 helices of nsp8 to form the dimerization interface of 1,340 Ų, formed nearly entirely by hydrophobic interactions<ref name="Konkolova"/>. | ||
| + | In the nsp7 of SARS-CoV-2 only one residue substitution is present when compared to SARS-CoV<ref name="Peng"/>. | ||
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| + | The to date published structures of complexes with nsp7 include 6BV2, 6WIQ, 6WQD, 7BW4, 6WTC, 6XEZ, 6M71, 7BV1, 7C2K, 7BZF, 6M5I, 6YHU, 6XIP, 6YYT, 7CTT, 6XQB, 6NUR, 7JLT, 2KYS, 7BTF, 5F22, 1YSY. | ||
== See also == | == See also == | ||
Revision as of 18:02, 28 September 2020
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References
- ↑ 1.0 1.1 1.2 Peng Q, Peng R, Yuan B, Zhao J, Wang M, Wang X, Wang Q, Sun Y, Fan Z, Qi J, Gao GF, Shi Y. Structural and Biochemical Characterization of the nsp12-nsp7-nsp8 Core Polymerase Complex from SARS-CoV-2. Cell Rep. 2020 Jun 16;31(11):107774. doi: 10.1016/j.celrep.2020.107774. Epub 2020, May 30. PMID:32531208 doi:http://dx.doi.org/10.1016/j.celrep.2020.107774
- ↑ 2.0 2.1 2.2 2.3 Konkolova E, Klima M, Nencka R, Boura E. Structural analysis of the putative SARS-CoV-2 primase complex. J Struct Biol. 2020 Aug 1;211(2):107548. doi: 10.1016/j.jsb.2020.107548. Epub, 2020 Jun 11. PMID:32535228 doi:http://dx.doi.org/10.1016/j.jsb.2020.107548
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