8fwp - Revision history

OCA at 10:48, 22 May 2024

2024-05-22T10:48:46Z

← Older revision		Revision as of 10:48, 22 May 2024
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	Septins, often described as the fourth component of the cytoskeleton, are structural proteins found in a vast variety of living beings. They are related to small GTPases and thus, generally, present GTPase activity which may play an important (although incompletely understood) role in their organization and function. Septins polymerize into long non-polar filaments, in which each subunit interacts with two others by alternating interfaces, NC and G. In Saccharomyces cerevisiae four septins are organized in the following manner, [Cdc11-Cdc12-Cdc3-Cdc10-Cdc10-Cdc3-Cdc12-Cdc11](n) in order to form filaments. Although septins were originally discovered in yeast and much is known regarding their biochemistry and function, only limited structural information about them is currently available. Here we present crystal structures of Cdc3/Cdc10 which provide the first view of the physiological interfaces formed by yeast septins. The G-interface has properties which place it in between that formed by SEPT2/SEPT6 and SEPT7/SEPT3 in human filaments. Switch I from Cdc10 contributes significantly to the interface, whereas in Cdc3 it is largely disorded. However, the significant negative charge density of the latter suggests it may have a unique role. At the NC-interface, we describe an elegant means by which the sidechain of a glutamine from helix alpha(0) imitates a peptide group in order to retain hydrogen-bond continuity at the kink between helices alpha(5) and alpha(6) in the neighbouring subunit, thereby justifying the conservation of the helical distortion. Its absence from Cdc11, along with this structure's other unusual features are critically discussed by comparison with Cdc3 and Cdc10.		Septins, often described as the fourth component of the cytoskeleton, are structural proteins found in a vast variety of living beings. They are related to small GTPases and thus, generally, present GTPase activity which may play an important (although incompletely understood) role in their organization and function. Septins polymerize into long non-polar filaments, in which each subunit interacts with two others by alternating interfaces, NC and G. In Saccharomyces cerevisiae four septins are organized in the following manner, [Cdc11-Cdc12-Cdc3-Cdc10-Cdc10-Cdc3-Cdc12-Cdc11](n) in order to form filaments. Although septins were originally discovered in yeast and much is known regarding their biochemistry and function, only limited structural information about them is currently available. Here we present crystal structures of Cdc3/Cdc10 which provide the first view of the physiological interfaces formed by yeast septins. The G-interface has properties which place it in between that formed by SEPT2/SEPT6 and SEPT7/SEPT3 in human filaments. Switch I from Cdc10 contributes significantly to the interface, whereas in Cdc3 it is largely disorded. However, the significant negative charge density of the latter suggests it may have a unique role. At the NC-interface, we describe an elegant means by which the sidechain of a glutamine from helix alpha(0) imitates a peptide group in order to retain hydrogen-bond continuity at the kink between helices alpha(5) and alpha(6) in the neighbouring subunit, thereby justifying the conservation of the helical distortion. Its absence from Cdc11, along with this structure's other unusual features are critically discussed by comparison with Cdc3 and Cdc10.

	A key piece of the puzzle: The central tetramer of the Saccharomyces cerevisiae septin protofilament and its implications for self-assembly.,Marques da Silva R, Christe Dos Reis Saladino G, Antonio Leonardo D, D'Muniz Pereira H, Andrea Sculaccio S, Paula Ulian Araujo A, Charles Garratt R J Struct Biol. 2023 ~~Jun 12~~;215(3):107983. doi: 10.1016/j.jsb.2023.107983. PMID:37315820<ref>PMID:37315820</ref>		A key piece of the puzzle: The central tetramer of the Saccharomyces cerevisiae septin protofilament and its implications for self-assembly.,Marques da Silva R, Christe Dos Reis Saladino G, Antonio Leonardo D, D'Muniz Pereira H, Andrea Sculaccio S, Paula Ulian Araujo A, Charles Garratt R J Struct Biol. 2023 Sep;215(3):107983. doi: 10.1016/j.jsb.2023.107983. Epub 2023 , Jun 12. PMID:37315820<ref>PMID:37315820</ref>

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

OCA at 05:45, 5 July 2023

2023-07-05T05:45:27Z

← Older revision		Revision as of 05:45, 5 July 2023
Line 1:		Line 1:
	~~'''Unreleased structure'''~~

	~~The entry~~ 8fwp is ~~ON HOLD~~ until ~~Paper~~ Publication		==Crystal Structure of CDC10 - CDC3 heterocomplex from Saccharomyces cerevisiae==
			<StructureSection load='8fwp' size='340' side='right'caption='[[8fwp]], [[Resolution\|resolution]] 2.22Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[8fwp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FWP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FWP FirstGlance]. <br>
			</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.22Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=8fwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fwp OCA], [https://pdbe.org/8fwp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fwp RCSB], [https://www.ebi.ac.uk/pdbsum/8fwp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fwp ProSAT]</span></td></tr>
			</table>
			== Function ==
			[https://www.uniprot.org/uniprot/CDC10_YEAST CDC10_YEAST] Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring approximate 15 minutes before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinases GIN4 and/or CLA4. May act by recruiting MYO1 and HOF1, a protein involved in septation, to the site of cleavage. Septins are also involved in cell morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation.
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Septins, often described as the fourth component of the cytoskeleton, are structural proteins found in a vast variety of living beings. They are related to small GTPases and thus, generally, present GTPase activity which may play an important (although incompletely understood) role in their organization and function. Septins polymerize into long non-polar filaments, in which each subunit interacts with two others by alternating interfaces, NC and G. In Saccharomyces cerevisiae four septins are organized in the following manner, [Cdc11-Cdc12-Cdc3-Cdc10-Cdc10-Cdc3-Cdc12-Cdc11](n) in order to form filaments. Although septins were originally discovered in yeast and much is known regarding their biochemistry and function, only limited structural information about them is currently available. Here we present crystal structures of Cdc3/Cdc10 which provide the first view of the physiological interfaces formed by yeast septins. The G-interface has properties which place it in between that formed by SEPT2/SEPT6 and SEPT7/SEPT3 in human filaments. Switch I from Cdc10 contributes significantly to the interface, whereas in Cdc3 it is largely disorded. However, the significant negative charge density of the latter suggests it may have a unique role. At the NC-interface, we describe an elegant means by which the sidechain of a glutamine from helix alpha(0) imitates a peptide group in order to retain hydrogen-bond continuity at the kink between helices alpha(5) and alpha(6) in the neighbouring subunit, thereby justifying the conservation of the helical distortion. Its absence from Cdc11, along with this structure's other unusual features are critically discussed by comparison with Cdc3 and Cdc10.

	~~Authors~~: Silva, ~~R.M.~~, Leonardo, D~~.A.~~, ~~Pereira~~, ~~H.M.~~, Garratt, R.C.		A key piece of the puzzle: The central tetramer of the Saccharomyces cerevisiae septin protofilament and its implications for self-assembly.,Marques da Silva R, Christe Dos Reis Saladino G, Antonio Leonardo D, D'Muniz Pereira H, Andrea Sculaccio S, Paula Ulian Araujo A, Charles Garratt R J Struct Biol. 2023 Jun 12;215(3):107983. doi: 10.1016/j.jsb.2023.107983. PMID:37315820<ref>PMID:37315820</ref>

	~~Description: Crystal Structure~~ of ~~CDC10~~ -~~CDC3 heterocomplex from Saccharomyces cerevisiae~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	[[Category: ~~Unreleased~~ Structures]]		</div>
	[[Category: Garratt~~, R.C~~]]		<div class="pdbe-citations 8fwp" style="background-color:#fffaf0;"></div>
	[[Category: ~~Pereira, H.M~~]]		== References ==
	[[Category: ~~Silva, R.M~~]]		<references/>
	[[Category: ~~Leonardo, D.A~~]]		__TOC__
			</StructureSection>
			[[Category: Large Structures]]
			[[Category: Saccharomyces cerevisiae S288C]]
			[[Category: Garratt RC]]
			[[Category: Leonardo DA]]
			[[Category: Pereira HM]]
			[[Category: Silva RM]]

OCA: Protected "8fwp" [edit=sysop:move=sysop]

2023-02-01T09:27:23Z

Protected "8fwp" [edit=sysop:move=sysop]

← Older revision	Revision as of 09:27, 1 February 2023
(No difference)

OCA: New page: '''Unreleased structure''' The entry 8fwp is ON HOLD until Paper Publication Authors: Silva, R.M., Leonardo, D.A., Pereira, H.M., Garratt, R.C. Description: Crystal Structure of CDC10 ...

2023-02-01T09:27:21Z

New page: '''Unreleased structure''' The entry 8fwp is ON HOLD until Paper Publication Authors: Silva, R.M., Leonardo, D.A., Pereira, H.M., Garratt, R.C. Description: Crystal Structure of CDC10 ...

New page

'''Unreleased structure'''

The entry 8fwp is ON HOLD until Paper Publication

Authors: Silva, R.M., Leonardo, D.A., Pereira, H.M., Garratt, R.C.

Description: Crystal Structure of CDC10 -CDC3 heterocomplex from Saccharomyces cerevisiae
[[Category: Unreleased Structures]]
[[Category: Garratt, R.C]]
[[Category: Pereira, H.M]]
[[Category: Silva, R.M]]
[[Category: Leonardo, D.A]]