2bl6

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of the Zn complex of EIAV NCp11(22-58) peptide, including two CCHC Zn-binding motifs.

Structural highlights

2bl6 is a 1 chain structure with sequence from Equine infectious anemia virus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GAG_EIAVY Matrix protein p15 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane (By similarity). Capsid protein p26 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity). Nucleocapsid protein p11 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity). p9 plays a role in budding of the assembled particle by interacting with PDCD6IP/AIP1 (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

Lentiviral nucleocapsid proteins are a class of multifunctional proteins that play an essential role in RNA packaging and viral infectivity. They contain two CX(2)CX(4)HX(4)C zinc binding motifs connected by a basic linker of variable length. The 3D structure of a 37-aa peptide corresponding to sequence 22-58 from lentiviral EIAV nucleocapsid protein NCp11, complexed with zinc, has been determined by 2D (1)H NMR spectroscopy, simulated annealing, and molecular dynamics. The solution structure consists of two zinc binding domains held together by a five-residue basic linker Arg(38)-Ala-Pro-Lys-Val(42) that allows for spatial proximity between the two finger domains. Observed linker folding is stabilized by H bonded secondary structure elements, resulting in an Omega-shaped central region, asymmetrically centered on the linker. The conformational differences and similarities with other NC zinc binding knuckles have been systematically analyzed. The two CCHC motifs, both characterized by a peculiar Pro-Gly sequence preceding the His residue, although preserving Zn-binding geometry and chirality of other known NC proteins, exhibit local fold differences both between each other and in comparison with other previously characterized retroviral CCHC motifs.

Structural features in EIAV NCp11: a lentivirus nucleocapsid protein with a short linker.,Amodeo P, Castiglione Morelli MA, Ostuni A, Battistuzzi G, Bavoso A Biochemistry. 2006 May 2;45(17):5517-26. PMID:16634633^[1]

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

References

↑ Amodeo P, Castiglione Morelli MA, Ostuni A, Battistuzzi G, Bavoso A. Structural features in EIAV NCp11: a lentivirus nucleocapsid protein with a short linker. Biochemistry. 2006 May 2;45(17):5517-26. PMID:16634633 doi:10.1021/bi0524924

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bl6"

@@ Line 1: / Line 1: @@
 ==Solution structure of the Zn complex of EIAV NCp11(22-58) peptide, including two CCHC Zn-binding motifs.==
-<StructureSection load='2bl6' size='340' side='right'caption='[[2bl6]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>
+<StructureSection load='2bl6' size='340' side='right'caption='[[2bl6]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2bl6]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BL6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2bl6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equine_infectious_anemia_virus Equine infectious anemia virus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BL6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1eia|1eia]], [[1hek|1hek]], [[2eia|2eia]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2bl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bl6 OCA], [https://pdbe.org/2bl6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bl6 RCSB], [https://www.ebi.ac.uk/pdbsum/2bl6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bl6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/GAG_EIAVY GAG_EIAVY]] Matrix protein p15 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane (By similarity).  Capsid protein p26 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity).  Nucleocapsid protein p11 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity).  p9 plays a role in budding of the assembled particle by interacting with PDCD6IP/AIP1 (By similarity).
+[https://www.uniprot.org/uniprot/GAG_EIAVY GAG_EIAVY] Matrix protein p15 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane (By similarity).  Capsid protein p26 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity).  Nucleocapsid protein p11 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity).  p9 plays a role in budding of the assembled particle by interacting with PDCD6IP/AIP1 (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 33: @@
 __TOC__
 </StructureSection>
+[[Category: Equine infectious anemia virus]]
 [[Category: Large Structures]]
-[[Category: Amodeo, P]]
+[[Category: Amodeo P]]
-[[Category: Bavoso, A]]
+[[Category: Bavoso A]]
-[[Category: Castiglione-Morelli, M A]]
+[[Category: Castiglione-Morelli MA]]
-[[Category: Ostuni, A]]
+[[Category: Ostuni A]]
-[[Category: Core protein]]
-[[Category: Lentivirus]]
-[[Category: Nucleocapsid protein]]
-[[Category: Polyprotein]]
-[[Category: Retrovirus zinc finger-like domain]]

2bl6

From Proteopedia

Current revision

Solution structure of the Zn complex of EIAV NCp11(22-58) peptide, including two CCHC Zn-binding motifs.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox