2fmx: Difference between revisions

Revision as of 14:51, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2fmx.png

Template:STRUCTURE 2fmx

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

Template:ABSTRACT PUBMED 16899220

About this StructureAbout this Structure

2FMX is a Single protein structure of sequence from Cricetulus griseus. Full crystallographic information is available from OCA.

ReferenceReference

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

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''An open conformation of switch I revealed by Sar1-GDP crystal structure at low Mg(2+)'''
+===An open conformation of switch I revealed by Sar1-GDP crystal structure at low Mg(2+)===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16899220}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16899220 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16899220}}
 ==About this Structure==
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 [[Category: Dimerization]]
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