2oaj

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Revision as of 07:04, 22 August 2018

Crystal structure of Sro7 from S. cerevisiae

Structural highlights

2oaj is a 1 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	SNI1, SRO7 (ATCC 18824)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SRO7_YEAST] Acts as an allosteric regulator of polarized exocytosis by promoting the targeted fusion of vesicles with the plasma membrane. Coordinates the spatial and temporal nature of both Rab-dependent tethering and SNARE-dependent membrane fusion of exocytic vesicles with the plasma membrane. Required for targeting of the sodium pumping ATPase ENA1 to the Cell Surface, thus being involved in maintenance of ion homeostasis in cells exposed to NaCl stress. May be involved in the targeting of the myosin proteins to their intrinsic pathways. Multicopy suppressor of RHO3. May also participate in the maintenance of cell polarity and bud growth.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

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

Polarized exocytosis requires coordination between the actin cytoskeleton and the exocytic machinery responsible for fusion of secretory vesicles at specific sites on the plasma membrane. Fusion requires formation of a complex between a vesicle-bound R-SNARE and plasma membrane Qa, Qb and Qc SNARE proteins. Proteins in the lethal giant larvae protein family, including lethal giant larvae and tomosyn in metazoans and Sro7 in yeast, interact with Q-SNAREs and are emerging as key regulators of polarized exocytosis. The crystal structure of Sro7 reveals two seven-bladed WD40 beta-propellers followed by a 60-residue-long 'tail', which is bound to the surface of the amino-terminal propeller. Deletion of the Sro7 tail enables binding to the Qbc SNARE region of Sec9 and this interaction inhibits SNARE complex assembly. The N-terminal domain of Sec9 provides a second, high-affinity Sro7 interaction that is unaffected by the tail. The results suggest that Sro7 acts as an allosteric regulator of exocytosis through interactions with factors that control the tail. Sequence alignments indicate that lethal giant larvae and tomosyn have a two-beta-propeller fold similar to that of Sro7, but only tomosyn appears to retain the regulatory tail.

Structure of the yeast polarity protein Sro7 reveals a SNARE regulatory mechanism.,Hattendorf DA, Andreeva A, Gangar A, Brennwald PJ, Weis WI Nature. 2007 Mar 29;446(7135):567-71. PMID:17392788^[8]

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

References

↑ Lehman K, Rossi G, Adamo JE, Brennwald P. Yeast homologues of tomosyn and lethal giant larvae function in exocytosis and are associated with the plasma membrane SNARE, Sec9. J Cell Biol. 1999 Jul 12;146(1):125-40. PMID:10402465
↑ Warringer J, Ericson E, Fernandez L, Nerman O, Blomberg A. High-resolution yeast phenomics resolves different physiological features in the saline response. Proc Natl Acad Sci U S A. 2003 Dec 23;100(26):15724-9. Epub 2003 Dec 15. PMID:14676322 doi:http://dx.doi.org/10.1073/pnas.2435976100
↑ Grosshans BL, Andreeva A, Gangar A, Niessen S, Yates JR 3rd, Brennwald P, Novick P. The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p. J Cell Biol. 2006 Jan 2;172(1):55-66. PMID:16390997 doi:http://dx.doi.org/10.1083/jcb.200510016
↑ Wadskog I, Forsmark A, Rossi G, Konopka C, Oyen M, Goksor M, Ronne H, Brennwald P, Adler L. The yeast tumor suppressor homologue Sro7p is required for targeting of the sodium pumping ATPase to the cell surface. Mol Biol Cell. 2006 Dec;17(12):4988-5003. Epub 2006 Sep 27. PMID:17005914 doi:http://dx.doi.org/10.1091/mbc.E05-08-0798
↑ Hattendorf DA, Andreeva A, Gangar A, Brennwald PJ, Weis WI. Structure of the yeast polarity protein Sro7 reveals a SNARE regulatory mechanism. Nature. 2007 Mar 29;446(7135):567-71. PMID:17392788 doi:10.1038/nature05635
↑ Rossi G, Brennwald P. Yeast homologues of lethal giant larvae and type V myosin cooperate in the regulation of Rab-dependent vesicle clustering and polarized exocytosis. Mol Biol Cell. 2011 Mar 15;22(6):842-57. doi: 10.1091/mbc.E10-07-0570. Epub 2011 , Jan 19. PMID:21248204 doi:http://dx.doi.org/10.1091/mbc.E10-07-0570
↑ Larsson K, Bohl F, Sjostrom I, Akhtar N, Strand D, Mechler BM, Grabowski R, Adler L. The Saccharomyces cerevisiae SOP1 and SOP2 genes, which act in cation homeostasis, can be functionally substituted by the Drosophila lethal(2)giant larvae tumor suppressor gene. J Biol Chem. 1998 Dec 11;273(50):33610-8. PMID:9837945
↑ Hattendorf DA, Andreeva A, Gangar A, Brennwald PJ, Weis WI. Structure of the yeast polarity protein Sro7 reveals a SNARE regulatory mechanism. Nature. 2007 Mar 29;446(7135):567-71. PMID:17392788 doi:10.1038/nature05635

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/2oaj"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Sro7 from S. cerevisiae==
 <StructureSection load='2oaj' size='340' side='right' caption='[[2oaj]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SNI1, SRO7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=2oaj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oaj OCA], [http://pdbe.org/2oaj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2oaj RCSB], [http://www.ebi.ac.uk/pdbsum/2oaj PDBsum]</span></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=2oaj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oaj OCA], [http://pdbe.org/2oaj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2oaj RCSB], [http://www.ebi.ac.uk/pdbsum/2oaj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2oaj ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oa/2oaj_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oa/2oaj_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2oaj

From Proteopedia

Revision as of 07:04, 22 August 2018

Crystal structure of Sro7 from S. cerevisiae

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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