6fsf

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the tandem PX-PH-domains of Bem3 from Saccharomyces cerevisiae

Structural highlights

6fsf is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BEM3_YEAST GTPase-activating protein (GAP) for CDC42 and less efficiently for RHO1. Negative regulator of the pheromone-response pathway through the STE20 protein kinase.^[1] ^[2]

Publication Abstract from PubMed

The structure of the tandem lipid-binding PX and pleckstrin-homology (PH) domains of the Cdc42 GTPase-activating protein Bem3 from Saccharomyces cerevisiae (strain S288c) has been determined to a resolution of 2.2 A (Rwork = 21.1%, Rfree = 23.4%). It shows that the domains adopt a relative orientation that enables them to simultaneously bind to a membrane and suggests possible cooperativity in membrane binding.

Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae.,Ali I, Eu S, Koch D, Bleimling N, Goody RS, Muller MP Acta Crystallogr F Struct Biol Commun. 2018 May 1;74(Pt 5):315-321. doi:, 10.1107/S2053230X18005915. Epub 2018 Apr 24. PMID:29718000^[3]

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

References

↑ Zheng Y, Hart MJ, Shinjo K, Evans T, Bender A, Cerione RA. Biochemical comparisons of the Saccharomyces cerevisiae Bem2 and Bem3 proteins. Delineation of a limit Cdc42 GTPase-activating protein domain. J Biol Chem. 1993 Nov 25;268(33):24629-34. PMID:8227021
↑ Zheng Y, Cerione R, Bender A. Control of the yeast bud-site assembly GTPase Cdc42. Catalysis of guanine nucleotide exchange by Cdc24 and stimulation of GTPase activity by Bem3. J Biol Chem. 1994 Jan 28;269(4):2369-72. PMID:8300560
↑ Ali I, Eu S, Koch D, Bleimling N, Goody RS, Muller MP. Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae. Acta Crystallogr F Struct Biol Commun. 2018 May 1;74(Pt 5):315-321. doi:, 10.1107/S2053230X18005915. Epub 2018 Apr 24. PMID:29718000 doi:http://dx.doi.org/10.1107/S2053230X18005915

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6fsf"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the tandem PX-PH-domains of Bem3 from Saccharomyces cerevisiae==
-<StructureSection load='6fsf' size='340' side='right' caption='[[6fsf]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='6fsf' size='340' side='right'caption='[[6fsf]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6fsf]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FSF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FSF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6fsf]] is a 1 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=6FSF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FSF FirstGlance]. <br>
-</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=6fsf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fsf OCA], [http://pdbe.org/6fsf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fsf RCSB], [http://www.ebi.ac.uk/pdbsum/6fsf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fsf ProSAT]</span></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]] 2.2&#8491;</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=6fsf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fsf OCA], [https://pdbe.org/6fsf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fsf RCSB], [https://www.ebi.ac.uk/pdbsum/6fsf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fsf ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/BEM3_YEAST BEM3_YEAST]] GTPase-activating protein (GAP) for CDC42 and less efficiently for RHO1. Negative regulator of the pheromone-response pathway through the STE20 protein kinase.<ref>PMID:8227021</ref> <ref>PMID:8300560</ref>
+[https://www.uniprot.org/uniprot/BEM3_YEAST BEM3_YEAST] GTPase-activating protein (GAP) for CDC42 and less efficiently for RHO1. Negative regulator of the pheromone-response pathway through the STE20 protein kinase.<ref>PMID:8227021</ref> <ref>PMID:8300560</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Ali, I]]
+[[Category: Large Structures]]
-[[Category: Bleimling, N]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Eu, S]]
+[[Category: Ali I]]
-[[Category: Goody, R S]]
+[[Category: Bleimling N]]
-[[Category: Koch, D]]
+[[Category: Eu S]]
-[[Category: Mueller, M P]]
+[[Category: Goody RS]]
-[[Category: Bem3]]
+[[Category: Koch D]]
-[[Category: Endocytosis]]
+[[Category: Mueller MP]]
-[[Category: Ph domain]]
-[[Category: Phosphatidylinositol phosphate]]
-[[Category: Phox]]
-[[Category: Pip]]
-[[Category: Pleckstrin homology]]
-[[Category: Px domain]]

6fsf

From Proteopedia

Current revision

Crystal structure of the tandem PX-PH-domains of Bem3 from Saccharomyces cerevisiae

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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