2fmx

From Proteopedia

(Difference between revisions)

Revision as of 16:06, 22 December 2021

An open conformation of switch I revealed by Sar1-GDP crystal structure at low Mg(2+)

Structural highlights

2fmx is a 2 chain structure with sequence from Cho cell lines. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	2fa9, 1f6b
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SAR1B_CRIGR] Involved in transport from the endoplasmic reticulum to the Golgi apparatus. Activated by the guanine nucleotide exchange factor PREB. Involved in the selection of the protein cargo and the assembly of the COPII coat complex.^[1] ^[2]

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

Mg2+ is essential for guanosine triphosphatase activity and plays key roles in guanine nucleotide binding and preserving the structural integrity of GTP-binding proteins. To understand the structural basis for Mg2+ function during the GDP/GTP exchange process, we determined the crystal structure of Delta9-Sar1-GDP at low Mg2+ concentration at 1.8A. Two Sar1-GDP molecules in the crystal form a dimer with Mg2+ presenting only in molecule B but not in molecule A. The absence of Mg2+ induces significant conformational changes in the switch I region in molecule A that shows similarities with those of Ha-Ras bound to Sos. The current structure reveals an important regulatory role for Mg2+. We suggest that guanine nucleotide exchange factor may utilize this feature to generate an open conformation for GDP/GTP exchange. Furthermore, we propose a mechanism for COPII assembly and disassembly in which dimerization of Sar1 plays an important role.

An open conformation of switch I revealed by Sar1-GDP crystal structure at low Mg2+.,Rao Y, Bian C, Yuan C, Li Y, Chen L, Ye X, Huang Z, Huang M Biochem Biophys Res Commun. 2006 Sep 29;348(3):908-15. Epub 2006 Aug 1. PMID:16899220^[3]

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

References

↑ Kuge O, Dascher C, Orci L, Rowe T, Amherdt M, Plutner H, Ravazzola M, Tanigawa G, Rothman JE, Balch WE. Sar1 promotes vesicle budding from the endoplasmic reticulum but not Golgi compartments. J Cell Biol. 1994 Apr;125(1):51-65. PMID:8138575
↑ Aridor M, Fish KN, Bannykh S, Weissman J, Roberts TH, Lippincott-Schwartz J, Balch WE. The Sar1 GTPase coordinates biosynthetic cargo selection with endoplasmic reticulum export site assembly. J Cell Biol. 2001 Jan 8;152(1):213-29. PMID:11149932
↑ Rao Y, Bian C, Yuan C, Li Y, Chen L, Ye X, Huang Z, Huang M. An open conformation of switch I revealed by Sar1-GDP crystal structure at low Mg2+. Biochem Biophys Res Commun. 2006 Sep 29;348(3):908-15. Epub 2006 Aug 1. PMID:16899220 doi:10.1016/j.bbrc.2006.07.148

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2fmx"

@@ Line 3: / Line 3: @@
 <StructureSection load='2fmx' size='340' side='right'caption='[[2fmx]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2fmx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cho_cell_lines Cho cell lines]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FMX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2fmx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cho_cell_lines Cho cell lines]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FMX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fa9|2fa9]], [[1f6b|1f6b]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2fa9|2fa9]], [[1f6b|1f6b]]</div></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=2fmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fmx OCA], [http://pdbe.org/2fmx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fmx RCSB], [http://www.ebi.ac.uk/pdbsum/2fmx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fmx 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=2fmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fmx OCA], [https://pdbe.org/2fmx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fmx RCSB], [https://www.ebi.ac.uk/pdbsum/2fmx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fmx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SAR1B_CRIGR SAR1B_CRIGR]] Involved in transport from the endoplasmic reticulum to the Golgi apparatus. Activated by the guanine nucleotide exchange factor PREB. Involved in the selection of the protein cargo and the assembly of the COPII coat complex.<ref>PMID:8138575</ref> <ref>PMID:11149932</ref>
+[[https://www.uniprot.org/uniprot/SAR1B_CRIGR SAR1B_CRIGR]] Involved in transport from the endoplasmic reticulum to the Golgi apparatus. Activated by the guanine nucleotide exchange factor PREB. Involved in the selection of the protein cargo and the assembly of the COPII coat complex.<ref>PMID:8138575</ref> <ref>PMID:11149932</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2fmx

From Proteopedia

Revision as of 16:06, 22 December 2021

An open conformation of switch I revealed by Sar1-GDP crystal structure at low Mg(2+)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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