1eq6: Difference between revisions
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==1.9 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE SACCHAROMYCES CEREVISIAE RAN-BINDING PROTEIN MOG1P== | ==1.9 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE SACCHAROMYCES CEREVISIAE RAN-BINDING PROTEIN MOG1P== | ||
<StructureSection load='1eq6' size='340' side='right' caption='[[1eq6]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1eq6' size='340' side='right' caption='[[1eq6]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1eq6]] is a 1 chain structure | <table><tr><td colspan='2'>[[1eq6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EQ6 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=1eq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eq6 OCA], [http://pdbe.org/1eq6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1eq6 RCSB], [http://www.ebi.ac.uk/pdbsum/1eq6 PDBsum]</span></td></tr> | </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=1eq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eq6 OCA], [http://pdbe.org/1eq6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1eq6 RCSB], [http://www.ebi.ac.uk/pdbsum/1eq6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1eq6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1eq6 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Baker, R P]] | [[Category: Baker, R P]] | ||
[[Category: Stewart, M]] | [[Category: Stewart, M]] | ||
[[Category: Alpha-beta]] | [[Category: Alpha-beta]] | ||
[[Category: Protein transport]] | [[Category: Protein transport]] | ||
Revision as of 06:58, 6 September 2017
1.9 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE SACCHAROMYCES CEREVISIAE RAN-BINDING PROTEIN MOG1P1.9 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE SACCHAROMYCES CEREVISIAE RAN-BINDING PROTEIN MOG1P
Structural highlights
Function[MOG1_YEAST] Involved in the Ran-GTPase system for nuclear protein import and poly(A)+ mRNA export.[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 PubMedThe 1.9 A resolution X-ray crystal structure of Ran-binding protein Mog1p shows that it has a unique fold based on a six-stranded antiparallel beta-sheet backed on both sides by an extensive alpha-helix. The topology of some elements of Mog1p secondary structure resemble a portion of nuclear transport factor 2 (NTF2), but the hydrophobic cavity and surrounding negatively charged residues that are important in the NTF2-RanGDP interaction are not conserved in Mog1p. In addition to binding RanGTP, Mog1p forms a 1:1 complex with RanGDP and so binds Ran independent of its nucleotide state. Mog1p and NTF2 compete for binding to RanGDP indicating that their binding sites on RanGDP are sufficiently close to prevent both proteins binding simultaneously. Although there may be some overlap between the Mog1p and NTF2 binding sites on RanGDP, these sites are not identical. Sequence analysis of Mog1p homologues from Schizosaccharomyces pombe, human, and Caenorhabditis elegans in the context of the Mog1p crystal structure indicates the presence of a cluster of highly conserved surface residues consistent with an interaction site for Ran. 1.9 A resolution crystal structure of the Saccharomyces cerevisiae Ran-binding protein Mog1p.,Stewart M, Baker RP J Mol Biol. 2000 May 26;299(1):213-23. PMID:10860733[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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