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==Structure of SARS-CoV-2 Main Protease bound to pyrithione zinc==
==Structure of SARS-CoV-2 Main Protease bound to pyrithione zinc==
<StructureSection load='7b83' size='340' side='right'caption='[[7b83]]' scene=''>
<StructureSection load='7b83' size='340' side='right'caption='[[7b83]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6yt8 6yt8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B83 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7B83 FirstGlance]. <br>
<table><tr><td colspan='2'>[[7b83]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/2019-ncov 2019-ncov]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6yt8 6yt8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B83 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B83 FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7b83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b83 OCA], [http://pdbe.org/7b83 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7b83 RCSB], [http://www.ebi.ac.uk/pdbsum/7b83 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7b83 ProSAT]</span></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PK8:9-oxa-7-thia-1-azonia-8$l^{2}-zincabicyclo[4.3.0]nona-1,3,5-triene'>PK8</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ORF1ab ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2697049 2019-nCoV])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7b83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b83 OCA], [https://pdbe.org/7b83 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b83 RCSB], [https://www.ebi.ac.uk/pdbsum/7b83 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b83 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/A0A6M4NAY4_SARS2 A0A6M4NAY4_SARS2]] Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.[ARBA:ARBA00002182]  Forms a hexadecamer with 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.[ARBA:ARBA00003443]  May participate in viral replication by acting as a ssRNA-binding protein.[ARBA:ARBA00002012]  May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses.[ARBA:ARBA00003115]  Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system.[ARBA:ARBA00002840]  Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.[ARBA:ARBA00002798]  Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium.[ARBA:ARBA00002960]  Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation.[ARBA:ARBA00002697]  Responsible for replication and transcription of the viral RNA genome.[ARBA:ARBA00003927]
==See Also==
*[[Virus protease 3D structures|Virus protease 3D structures]]
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</StructureSection>
</StructureSection>
[[Category: 2019-ncov]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Alves Franca B]]
[[Category: Awel, S]]
[[Category: Awel S]]
[[Category: Beck, T]]
[[Category: Beck T]]
[[Category: Betzel, C]]
[[Category: Betzel C]]
[[Category: Brehm, W]]
[[Category: Brehm W]]
[[Category: Brognaro, H]]
[[Category: Brognaro H]]
[[Category: Chapman, H N]]
[[Category: Chapman HN]]
[[Category: Chari, A]]
[[Category: Chari A]]
[[Category: Domaracky, M]]
[[Category: Domaracky M]]
[[Category: Doyle, J J]]
[[Category: Doyle JJ]]
[[Category: Dunkel, I]]
[[Category: Dunkel I]]
[[Category: Ehrt, C]]
[[Category: Ehrt C]]
[[Category: Ellinger, B]]
[[Category: Ellinger B]]
[[Category: Esperanza, G Pena]]
[[Category: Falke S]]
[[Category: Falke, S]]
[[Category: Feiler C]]
[[Category: Feiler, C]]
[[Category: Fernandez Garcia Y]]
[[Category: Fischer, P]]
[[Category: Fischer P]]
[[Category: Fleckenstein, H]]
[[Category: Fleckenstein H]]
[[Category: Franca, B Alves]]
[[Category: Galchenkova M]]
[[Category: Galchenkova, M]]
[[Category: Gelisio L]]
[[Category: Garcia, Y Fernandez]]
[[Category: Gevorkov Y]]
[[Category: Gelisio, L]]
[[Category: Ginn H]]
[[Category: Gevorkov, Y]]
[[Category: Giseler H]]
[[Category: Ginn, H]]
[[Category: Gribbon P]]
[[Category: Giseler, H]]
[[Category: Groessler M]]
[[Category: Gribbon, P]]
[[Category: Guenther S]]
[[Category: Groessler, M]]
[[Category: Hakanpaeae J]]
[[Category: Guenther, S]]
[[Category: Han H]]
[[Category: Hakanpaeae, J]]
[[Category: Hennicke V]]
[[Category: Han, H]]
[[Category: Hilgenfeld R]]
[[Category: Hennicke, V]]
[[Category: Knoska J]]
[[Category: Hilgenfeld, R]]
[[Category: Koua F]]
[[Category: Knoska, J]]
[[Category: Kuzikov M]]
[[Category: Koua, F]]
[[Category: Lane TJ]]
[[Category: Kuzikov, M]]
[[Category: Li C]]
[[Category: Lane, T J]]
[[Category: Lieske J]]
[[Category: Li, C]]
[[Category: Lorenzen K]]
[[Category: Lieske, J]]
[[Category: Meents A]]
[[Category: Lorenzen, K]]
[[Category: Mehrabi P]]
[[Category: Mashour, A Rahmani]]
[[Category: Meier S]]
[[Category: Meents, A]]
[[Category: Melo D]]
[[Category: Mehrabi, P]]
[[Category: Meyer J]]
[[Category: Meier, S]]
[[Category: Noei H]]
[[Category: Melo, D]]
[[Category: Norton-Baker B]]
[[Category: Meyer, J]]
[[Category: Oberthuer D]]
[[Category: Noei, H]]
[[Category: Paulraj LX]]
[[Category: Norton-Baker, B]]
[[Category: Pearson A]]
[[Category: Oberthuer, D]]
[[Category: Peck A]]
[[Category: Paulraj, L X]]
[[Category: Pena Esperanza G]]
[[Category: Pearson, A]]
[[Category: Perbandt M]]
[[Category: Peck, A]]
[[Category: Pletzer-Zelgert J]]
[[Category: Perbandt, M]]
[[Category: Rahmani Mashour A]]
[[Category: Pletzer-Zelgert, J]]
[[Category: Rarey M]]
[[Category: Rarey, M]]
[[Category: Reinke P]]
[[Category: Reinke, P]]
[[Category: Saouane S]]
[[Category: Saouane, S]]
[[Category: Schmidt C]]
[[Category: Schmidt, C]]
[[Category: Schubert R]]
[[Category: Schubert, R]]
[[Category: Schulz EC]]
[[Category: Schulz, E C]]
[[Category: Schwinzer M]]
[[Category: Schwinzer, M]]
[[Category: Seychell B]]
[[Category: Seychell, B]]
[[Category: Tidow H]]
[[Category: Tidow, H]]
[[Category: Tolstikova A]]
[[Category: Tolstikova, A]]
[[Category: Trost F]]
[[Category: Trost, F]]
[[Category: Turk D]]
[[Category: Turk, D]]
[[Category: Ullah N]]
[[Category: Ullah, N]]
[[Category: Weiss M]]
[[Category: Weiss, M]]
[[Category: Werner N]]
[[Category: Werner, N]]
[[Category: White TA]]
[[Category: White, T A]]
[[Category: Wolf M]]
[[Category: Wolf, M]]
[[Category: Wollenhaupt J]]
[[Category: Wollenhaupt, J]]
[[Category: Yefanov O]]
[[Category: Yefanov, O]]
[[Category: Zaliani A]]
[[Category: Zaliani, A]]
[[Category: Zhang L]]
[[Category: Zhang, L]]
[[Category: Covid-!9]]
[[Category: Mpro]]
[[Category: Peptide binding protein]]
[[Category: Sars-cov-2]]

Revision as of 20:55, 10 March 2021

Structure of SARS-CoV-2 Main Protease bound to pyrithione zincStructure of SARS-CoV-2 Main Protease bound to pyrithione zinc

Structural highlights

7b83 is a 1 chain structure with sequence from 2019-ncov. This structure supersedes the now removed PDB entry 6yt8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
Gene:ORF1ab (2019-nCoV)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[A0A6M4NAY4_SARS2] Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.[ARBA:ARBA00002182] Forms a hexadecamer with 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.[ARBA:ARBA00003443] May participate in viral replication by acting as a ssRNA-binding protein.[ARBA:ARBA00002012] May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses.[ARBA:ARBA00003115] Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system.[ARBA:ARBA00002840] Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.[ARBA:ARBA00002798] Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium.[ARBA:ARBA00002960] Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation.[ARBA:ARBA00002697] Responsible for replication and transcription of the viral RNA genome.[ARBA:ARBA00003927]

See Also

7b83, resolution 1.80Å

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