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3g21

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Revision as of 07:25, 5 December 2018

Crystal structure of the C-terminal domain of the Rous Sarcoma Virus capsid protein: Low pH

Structural highlights

3g21 is a 1 chain structure with sequence from Rsv-prc. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3g0v, 3g1g, 3g1i, 3g26, 3g28, 3g29
Gene:	gag (RSV-PrC)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GAG_RSVP] Capsid protein p27 forms the spherical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity). The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell (By similarity).

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 PubMed

In mature retroviral particles, the capsid protein (CA) forms a shell encasing the viral replication complex. Human immunodeficiency virus (HIV) CA dimerizes in solution, through its C-terminal domain (CTD), and this interaction is important for capsid assembly. In contrast, other retroviral capsid proteins, including that of Rous sarcoma virus (RSV), do not dimerize with measurable affinity. Here we show, using X-ray crystallography and other biophysical methods, that acidification causes RSV CA to dimerize in a fashion analogous to HIV CA, and that this drives capsid assembly in vitro. A pair of aspartic acid residues, located within the CTD dimer interface, explains why dimerization is linked to proton binding. Our results show that despite overarching structural similarities, the intermolecular forces responsible for forming and stabilizing the retroviral capsid differ markedly across retroviral genera. Our data further suggest that proton binding may regulate RSV capsid assembly, or modulate stability of the assembled capsid.

Proton-linked dimerization of a retroviral capsid protein initiates capsid assembly.,Bailey GD, Hyun JK, Mitra AK, Kingston RL Structure. 2009 May 13;17(5):737-48. PMID:19446529^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bailey GD, Hyun JK, Mitra AK, Kingston RL. Proton-linked dimerization of a retroviral capsid protein initiates capsid assembly. Structure. 2009 May 13;17(5):737-48. PMID:19446529 doi:10.1016/j.str.2009.03.010

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3g21"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the C-terminal domain of the Rous Sarcoma Virus capsid protein: Low pH==
 <StructureSection load='3g21' size='340' side='right' caption='[[3g21]], [[Resolution|resolution]] 0.90&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3g0v|3g0v]], [[3g1g|3g1g]], [[3g1i|3g1i]], [[3g26|3g26]], [[3g28|3g28]], [[3g29|3g29]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gag ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11888 RSV-PrC])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3g21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g21 OCA], [http://pdbe.org/3g21 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g21 RCSB], [http://www.ebi.ac.uk/pdbsum/3g21 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3g21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g21 OCA], [http://pdbe.org/3g21 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g21 RCSB], [http://www.ebi.ac.uk/pdbsum/3g21 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3g21 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g2/3g21_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g2/3g21_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

3g21

From Proteopedia

Revision as of 07:25, 5 December 2018

Crystal structure of the C-terminal domain of the Rous Sarcoma Virus capsid protein: Low pH

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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