1cxq

From Proteopedia

(Difference between revisions)

Revision as of 10:41, 14 July 2021

ATOMIC RESOLUTION ASV INTEGRASE CORE DOMAIN FROM AMMONIUM SULFATE

Structural highlights

1cxq is a 1 chain structure with sequence from Avian sarcoma virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1asv, 1cxu, 1cz9, 1czb
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[POL_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

Six crystal structures of the core domain of integrase (IN) from avian sarcoma virus (ASV) and its active-site derivative containing an Asp64 --> Asn substitution have been solved at atomic resolution ranging 1.02-1.42 A. The high-quality data provide new structural information about the active site of the enzyme and clarify previous inconsistencies in the description of this fragment. The very high resolution of the data and excellent quality of the refined models explain the dynamic properties of IN and the multiple conformations of its disordered residues. They also allow an accurate description of the solvent structure and help to locate other molecules bound to the enzyme. A detailed analysis of the flexible active-site region, in particular the loop formed by residues 144-154, suggests conformational changes which may be associated with substrate binding and enzymatic activity. The pH-dependent conformational changes of the active-site loop correlates with the pH vs activity profile observed for ASV IN.

Atomic resolution structures of the core domain of avian sarcoma virus integrase and its D64N mutant.,Lubkowski J, Dauter Z, Yang F, Alexandratos J, Merkel G, Skalka AM, Wlodawer A Biochemistry. 1999 Oct 12;38(41):13512-22. PMID:10521258^[1]

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

References

↑ Lubkowski J, Dauter Z, Yang F, Alexandratos J, Merkel G, Skalka AM, Wlodawer A. Atomic resolution structures of the core domain of avian sarcoma virus integrase and its D64N mutant. Biochemistry. 1999 Oct 12;38(41):13512-22. PMID:10521258

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/1cxq"

@@ Line 3: / Line 3: @@
 <StructureSection load='1cxq' size='340' side='right'caption='[[1cxq]], [[Resolution|resolution]] 1.02&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1cxq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Avian_sarcoma_virus Avian sarcoma virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CXQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CXQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1cxq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Avian_sarcoma_virus Avian sarcoma virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CXQ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1asv|1asv]], [[1cxu|1cxu]], [[1cz9|1cz9]], [[1czb|1czb]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1asv|1asv]], [[1cxu|1cxu]], [[1cz9|1cz9]], [[1czb|1czb]]</div></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=1cxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cxq OCA], [http://pdbe.org/1cxq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cxq RCSB], [http://www.ebi.ac.uk/pdbsum/1cxq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cxq ProSAT]</span></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=1cxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cxq OCA], [https://pdbe.org/1cxq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cxq RCSB], [https://www.ebi.ac.uk/pdbsum/1cxq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cxq ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/POL_RSVP POL_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).
+[[https://www.uniprot.org/uniprot/POL_RSVP POL_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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Retroviral Integrase|Retroviral Integrase]]
+*[[Retroviral integrase 3D structures|Retroviral integrase 3D structures]]
 == References ==
 <references/>

1cxq

From Proteopedia

Revision as of 10:41, 14 July 2021

ATOMIC RESOLUTION ASV INTEGRASE CORE DOMAIN FROM AMMONIUM SULFATE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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