2kgf: Difference between revisions
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< | ==N-terminal domain of capsid protein from the Mason-Pfizer monkey virus== | ||
<StructureSection load='2kgf' size='340' side='right'caption='[[2kgf]]' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2kgf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mason-Pfizer_monkey_virus Mason-Pfizer monkey virus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KGF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KGF FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2kgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kgf OCA], [https://pdbe.org/2kgf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kgf RCSB], [https://www.ebi.ac.uk/pdbsum/2kgf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kgf ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/GAG_MPMV GAG_MPMV] p10 is the matrix protein. P14 is the nucleocapsid protein. p27 is the capsid protein. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kg/2kgf_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2kgf ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The high-resolution structure of the N-terminal domain (NTD) of the retroviral capsid protein (CA) of Mason-Pfizer monkey virus (M-PMV), a member of the betaretrovirus family, has been determined by NMR. The M-PMV NTD CA structure is similar to the other retroviral capsid structures and is characterized by a six alpha-helix bundle and an N-terminal beta-hairpin, stabilized by an interaction of highly conserved residues, Pro1 and Asp57. Since the role of the beta-hairpin has been shown to be critical for formation of infectious viral core, we also investigated the functional role of M-PMV beta-hairpin in two mutants (i.e., DeltaP1NTDCA and D57ANTDCA) where the salt bridge stabilizing the wild-type structure was disrupted. NMR data obtained for these mutants were compared with those obtained for the wild type. The main structural changes were observed within the beta-hairpin structure; within helices 2, 3, and 5; and in the loop connecting helices 2 and 3. This observation is supported by biochemical data showing different cleavage patterns of the wild-type and the mutated capsid-nucleocapsid fusion protein (CANC) by M-PMV protease. Despite these structural changes, the mutants with disrupted salt bridge are still able to assemble into immature, spherical particles. This confirms that the mutual interaction and topology within the beta-hairpin and helix 3 might correlate with the changes in interaction between immature and mature lattices. | |||
NMR structure of the N-terminal domain of capsid protein from the mason-pfizer monkey virus.,Macek P, Chmelik J, Krizova I, Kaderavek P, Padrta P, Zidek L, Wildova M, Hadravova R, Chaloupkova R, Pichova I, Ruml T, Rumlova M, Sklenar V J Mol Biol. 2009 Sep 11;392(1):100-14. Epub 2009 Jun 13. PMID:19527730<ref>PMID:19527730</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2kgf" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[ | [[Category: Mason-Pfizer monkey virus]] | ||
[[Category: Chmelik J]] | |||
== | [[Category: Kaderavek P]] | ||
< | [[Category: Macek P]] | ||
[[Category: Mason- | [[Category: Padrta P]] | ||
[[Category: Chmelik | [[Category: Pichova I]] | ||
[[Category: Kaderavek | [[Category: Ruml T]] | ||
[[Category: Macek | [[Category: Rumlova M]] | ||
[[Category: Padrta | [[Category: Sklenar V]] | ||
[[Category: Pichova | [[Category: Zidek L]] | ||
[[Category: Ruml | |||
[[Category: Rumlova | |||
[[Category: Sklenar | |||
[[Category: Zidek | |||
Latest revision as of 22:11, 29 May 2024
N-terminal domain of capsid protein from the Mason-Pfizer monkey virusN-terminal domain of capsid protein from the Mason-Pfizer monkey virus
Structural highlights
FunctionGAG_MPMV p10 is the matrix protein. P14 is the nucleocapsid protein. p27 is the capsid protein. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe high-resolution structure of the N-terminal domain (NTD) of the retroviral capsid protein (CA) of Mason-Pfizer monkey virus (M-PMV), a member of the betaretrovirus family, has been determined by NMR. The M-PMV NTD CA structure is similar to the other retroviral capsid structures and is characterized by a six alpha-helix bundle and an N-terminal beta-hairpin, stabilized by an interaction of highly conserved residues, Pro1 and Asp57. Since the role of the beta-hairpin has been shown to be critical for formation of infectious viral core, we also investigated the functional role of M-PMV beta-hairpin in two mutants (i.e., DeltaP1NTDCA and D57ANTDCA) where the salt bridge stabilizing the wild-type structure was disrupted. NMR data obtained for these mutants were compared with those obtained for the wild type. The main structural changes were observed within the beta-hairpin structure; within helices 2, 3, and 5; and in the loop connecting helices 2 and 3. This observation is supported by biochemical data showing different cleavage patterns of the wild-type and the mutated capsid-nucleocapsid fusion protein (CANC) by M-PMV protease. Despite these structural changes, the mutants with disrupted salt bridge are still able to assemble into immature, spherical particles. This confirms that the mutual interaction and topology within the beta-hairpin and helix 3 might correlate with the changes in interaction between immature and mature lattices. NMR structure of the N-terminal domain of capsid protein from the mason-pfizer monkey virus.,Macek P, Chmelik J, Krizova I, Kaderavek P, Padrta P, Zidek L, Wildova M, Hadravova R, Chaloupkova R, Pichova I, Ruml T, Rumlova M, Sklenar V J Mol Biol. 2009 Sep 11;392(1):100-14. Epub 2009 Jun 13. PMID:19527730[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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