2c03: Difference between revisions
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<StructureSection load='2c03' size='340' side='right' caption='[[2c03]], [[Resolution|resolution]] 1.24Å' scene=''> | <StructureSection load='2c03' size='340' side='right' caption='[[2c03]], [[Resolution|resolution]] 1.24Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2c03]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2c03]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25104 Atcc 25104]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C03 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C03 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ffh|1ffh]], [[1jpj|1jpj]], [[1jpn|1jpn]], [[1ls1|1ls1]], [[1ng1|1ng1]], [[1o87|1o87]], [[1okk|1okk]], [[1rj9|1rj9]], [[1ry1|1ry1]], [[2bqs|2bqs]], [[2bqt|2bqt]], [[2c04|2c04]], [[2ffh|2ffh]], [[2ng1|2ng1]], [[3ng1|3ng1]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ffh|1ffh]], [[1jpj|1jpj]], [[1jpn|1jpn]], [[1ls1|1ls1]], [[1ng1|1ng1]], [[1o87|1o87]], [[1okk|1okk]], [[1rj9|1rj9]], [[1ry1|1ry1]], [[2bqs|2bqs]], [[2bqt|2bqt]], [[2c04|2c04]], [[2ffh|2ffh]], [[2ng1|2ng1]], [[3ng1|3ng1]]</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=2c03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c03 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c03 RCSB], [http://www.ebi.ac.uk/pdbsum/2c03 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=2c03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c03 OCA], [http://pdbe.org/2c03 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c03 RCSB], [http://www.ebi.ac.uk/pdbsum/2c03 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2c03" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Atcc 25104]] | ||
[[Category: Freymann, D M]] | [[Category: Freymann, D M]] | ||
[[Category: Preininger, A M]] | [[Category: Preininger, A M]] | ||
Revision as of 15:43, 11 September 2015
GDP COMPLEX OF SRP GTPASE FFH NG DOMAINGDP COMPLEX OF SRP GTPASE FFH NG DOMAIN
Structural highlights
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 PubMedTwo structures of the nucleotide-bound NG domain of Ffh, the GTPase subunit of the bacterial signal recognition particle (SRP), have been determined at ultrahigh resolution in similar crystal forms. One is GDP-bound and one is GMPPCP-bound. The asymmetric unit of each structure contains two protein monomers, each of which exhibits differences in nucleotide-binding conformation and occupancy. The GDP-bound Ffh NG exhibits two binding conformations in one monomer but not the other and the GMPPCP-bound protein exhibits full occupancy of the nucleotide in one monomer but only partial occupancy in the other. Thus, under the same solution conditions, each crystal reveals multiple binding states that suggest that even when nucleotide is bound its position in the Ffh NG active site is dynamic. Some differences in the positioning of the bound nucleotide may arise from differences in the crystal-packing environment and specific factors that have been identified include the relative positions of the N and G domains, small conformational changes in the P-loop, the positions of waters buried within the active site and shifts in the closing loop that packs against the guanine base. However, ;loose' binding may have biological significance in promoting facile nucleotide exchange and providing a mechanism for priming the SRP GTPase prior to its activation in its complex with the SRP receptor. Nucleotide-binding flexibility in ultrahigh-resolution structures of the SRP GTPase Ffh.,Ramirez UD, Focia PJ, Freymann DM Acta Crystallogr D Biol Crystallogr. 2008 Oct;64(Pt 10):1043-53. Epub 2008, Sep 19. PMID:18931411[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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