1if0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:34, 7 February 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 3: Line 3:
<SX load='1if0' size='340' side='right' viewer='molstar' caption='[[1if0]], [[Resolution|resolution]] 12.00&Aring;' scene=''>
<SX load='1if0' size='340' side='right' viewer='molstar' caption='[[1if0]], [[Resolution|resolution]] 12.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1if0]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Bphk7 Bphk7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IF0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IF0 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1if0]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_HK97 Escherichia virus HK97]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IF0 FirstGlance]. <br>
-
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fh6|1fh6]]</td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 12&#8491;</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=1if0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1if0 OCA], [http://pdbe.org/1if0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1if0 RCSB], [http://www.ebi.ac.uk/pdbsum/1if0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1if0 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=1if0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1if0 OCA], [https://pdbe.org/1if0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1if0 RCSB], [https://www.ebi.ac.uk/pdbsum/1if0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1if0 ProSAT]</span></td></tr>
</table>
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/CAPSD_BPHK7 CAPSD_BPHK7] Assembles to form an icosahedral capsid of 66 nm, with a T=7 laevo symmetry (PubMed:11000116, PubMed:21276801). Responsible for its self-assembly into a procapsid. The phage does not need to encode a separate scaffolfing protein because its capsid protein contains the delta domain that carries that function.<ref>PMID:11000116</ref> <ref>PMID:21276801</ref> <ref>PMID:7669350</ref> <ref>PMID:7723020</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 17: Line 19:
</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=1if0 ConSurf].
</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=1if0 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
-
<div style="background-color:#fffaf0;">
 
-
== Publication Abstract from PubMed ==
 
-
Large-scale conformational changes transform viral precursors into infectious virions. The structure of bacteriophage HK97 capsid, Head-II, was recently solved by crystallography, revealing a catenated cross-linked topology. We have visualized its precursor, Prohead-II, by cryoelectron microscopy and modeled the conformational change by appropriately adapting Head-II. Rigid-body rotations ( approximately 40 degrees) cause switching to an entirely different set of interactions; in addition, two motifs undergo refolding. These changes stabilize the capsid by increasing the surface area buried at interfaces and bringing the cross-link-forming residues, initially approximately 40 angstroms apart, close together. The inner surface of Prohead-II is negatively charged, suggesting that the transition is triggered electrostatically by DNA packaging.
 
- 
-
Virus maturation involving large subunit rotations and local refolding.,Conway JF, Wikoff WR, Cheng N, Duda RL, Hendrix RW, Johnson JE, Steven AC Science. 2001 Apr 27;292(5517):744-8. PMID:11326105<ref>PMID:11326105</ref>
 
- 
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
-
</div>
 
-
<div class="pdbe-citations 1if0" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</SX>
</SX>
-
[[Category: Bphk7]]
+
[[Category: Escherichia virus HK97]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Cheng, N]]
+
[[Category: Cheng N]]
-
[[Category: Conway, J F]]
+
[[Category: Conway JF]]
-
[[Category: Duda, R L]]
+
[[Category: Duda RL]]
-
[[Category: Hendrix, R W]]
+
[[Category: Hendrix RW]]
-
[[Category: Johnson, J E]]
+
[[Category: Johnson JE]]
-
[[Category: Steven, A C]]
+
[[Category: Steven AC]]
-
[[Category: Wikoff, W R]]
+
[[Category: Wikoff WR]]
-
[[Category: Bacteriophage]]
+
-
[[Category: Capsid]]
+
-
[[Category: Cryoem]]
+
-
[[Category: Icosahedral virus]]
+
-
[[Category: Pseudo-atomic model]]
+
-
[[Category: Virus]]
+

Current revision

PSEUDO-ATOMIC MODEL OF BACTERIOPHAGE HK97 PROCAPSID (PROHEAD II)

1if0, resolution 12.00Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools