3oa7: Difference between revisions

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<StructureSection load='3oa7' size='340' side='right'caption='[[3oa7]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3oa7' size='340' side='right'caption='[[3oa7]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3oa7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpph2 Bpph2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OA7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OA7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3oa7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_virus_phi29 Bacillus virus phi29] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OA7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OA7 FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">7, CNM67, YNL225C, N1264 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10756 BPPH2])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3oa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oa7 OCA], [https://pdbe.org/3oa7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oa7 RCSB], [https://www.ebi.ac.uk/pdbsum/3oa7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oa7 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=3oa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oa7 OCA], [https://pdbe.org/3oa7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oa7 RCSB], [https://www.ebi.ac.uk/pdbsum/3oa7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oa7 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/SCAF_BPPH2 SCAF_BPPH2] Scaffolding protein involved in the icosahedric procapsid assembly. Coassembles with the capsid proteins to form the procapsid, in which the scaffolding protein is found within the external shell of icosahedrally arranged capsid protein subunits. In a subsequent step the scaffolding protein molecules are released from the procapsid.<ref>PMID:17098197</ref> <ref>PMID:17198713</ref> <ref>PMID:23896641</ref> [https://www.uniprot.org/uniprot/CNM67_YEAST CNM67_YEAST] Involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation. Required for the proper formation of the spindle pole body (SPB) outer plaque. May connect the outer plaque to the central plaque embedded in the nuclear envelope.<ref>PMID:11514632</ref> <ref>PMID:9571234</ref>  
The spindle pole body of the budding yeast Saccharomyces cerevisiae has served as a model system for understanding microtubule organizing centers, yet very little is known about the molecular structure of its components. We report here the structure of the C-terminal domain of the core component Cnm67 at 2.3 A resolution. The structure determination was aided by a novel approach to crystallization of proteins containing coiled-coils that utilizes globular domains to stabilize the coiled-coils. This enhances their solubility in Escherichia coli and improves their crystallization. The Cnm67 C-terminal domain (residues Asn-429-Lys-581) exhibits a previously unseen dimeric, interdigitated, all alpha-helical fold. In vivo studies demonstrate that this domain alone is able to localize to the spindle pole body. In addition, the structure reveals a large functionally indispensable positively charged surface patch that is implicated in spindle pole body localization. Finally, the C-terminal eight residues are disordered but are critical for protein folding and structural stability.
 
Structure-function analysis of the C-terminal domain of CNM67, a core component of the Saccharomyces cerevisiae spindle pole body.,Klenchin VA, Frye JJ, Jones MH, Winey M, Rayment I J Biol Chem. 2011 May 20;286(20):18240-50. Epub 2011 Mar 24. PMID:21454609<ref>PMID:21454609</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3oa7" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bpph2]]
[[Category: Bacillus virus phi29]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Frye, J J]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Klenchin, V A]]
[[Category: Frye JJ]]
[[Category: Rayment, I]]
[[Category: Klenchin VA]]
[[Category: Coiled coil]]
[[Category: Rayment I]]
[[Category: Spindle pole body]]
[[Category: Structural protein]]

Revision as of 13:04, 14 February 2024

Structure of the C-terminal domain of Cnm67, a core component of the spindle pole body of Saccharomyces cerevisiaeStructure of the C-terminal domain of Cnm67, a core component of the spindle pole body of Saccharomyces cerevisiae

Structural highlights

3oa7 is a 1 chain structure with sequence from Bacillus virus phi29 and Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SCAF_BPPH2 Scaffolding protein involved in the icosahedric procapsid assembly. Coassembles with the capsid proteins to form the procapsid, in which the scaffolding protein is found within the external shell of icosahedrally arranged capsid protein subunits. In a subsequent step the scaffolding protein molecules are released from the procapsid.[1] [2] [3] CNM67_YEAST Involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation. Required for the proper formation of the spindle pole body (SPB) outer plaque. May connect the outer plaque to the central plaque embedded in the nuclear envelope.[4] [5]

References

  1. ↑ Choi KH, Morais MC, Anderson DL, Rossmann MG. Determinants of bacteriophage phi29 head morphology. Structure. 2006 Nov;14(11):1723-7. PMID:17098197 doi:http://dx.doi.org/10.1016/j.str.2006.09.007
  2. ↑ Fu CY, Morais MC, Battisti AJ, Rossmann MG, Prevelige PE Jr. Molecular dissection of o29 scaffolding protein function in an in vitro assembly system. J Mol Biol. 2007 Mar 2;366(4):1161-73. Epub 2006 Dec 6. PMID:17198713 doi:http://dx.doi.org/10.1016/j.jmb.2006.11.091
  3. ↑ Li R, Cherwa JE Jr, Prevelige PE Jr. varphi29 Scaffolding and connector structure-function relationship studied by trans-complementation. Virology. 2013 Sep;444(1-2):355-62. doi: 10.1016/j.virol.2013.07.001. Epub 2013, Jul 27. PMID:23896641 doi:http://dx.doi.org/10.1016/j.virol.2013.07.001
  4. ↑ Schaerer F, Morgan G, Winey M, Philippsen P. Cnm67p is a spacer protein of the Saccharomyces cerevisiae spindle pole body outer plaque. Mol Biol Cell. 2001 Aug;12(8):2519-33. PMID:11514632 doi:10.1091/mbc.12.8.2519
  5. ↑ Brachat A, Kilmartin JV, Wach A, Philippsen P. Saccharomyces cerevisiae cells with defective spindle pole body outer plaques accomplish nuclear migration via half-bridge-organized microtubules. Mol Biol Cell. 1998 May;9(5):977-91. PMID:9571234 doi:10.1091/mbc.9.5.977

3oa7, resolution 2.30Å

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