24io: Difference between revisions
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==Crystal structure of the RelSeq N-terminal domain from Streptococcus equisimilis in complex with pppGpp== | |||
<StructureSection load='24io' size='340' side='right'caption='[[24io]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[24io]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_dysgalactiae_subsp._equisimilis Streptococcus dysgalactiae subsp. equisimilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=24IO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=24IO FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</td></tr> | |||
[[Category: | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0O2:GUANOSINE+5-(TETRAHYDROGEN+TRIPHOSPHATE)+3-(TRIHYDROGEN+DIPHOSPHATE)'>0O2</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | ||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=24io FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=24io OCA], [https://pdbe.org/24io PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=24io RCSB], [https://www.ebi.ac.uk/pdbsum/24io PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=24io ProSAT]</span></td></tr> | ||
[[Category: | </table> | ||
[[Category: Kasatsky | == Function == | ||
[[Category: | [https://www.uniprot.org/uniprot/RELA_STREQ RELA_STREQ] In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes both the formation of pppGpp which is then hydrolyzed to form ppGpp, and the hydrolysis of ppGpp. The enzyme does not similtaneously display both synthase and hydrolase activities. In the structure of residues 1-385 there are 2 conformations seen, the hydrolase-OFF/synthase-ON and hydrolase-ON/synthase-OFF, suggesting there is ligand-induced signal transmission between the 2 active sites. | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Streptococcus dysgalactiae subsp. equisimilis]] | |||
[[Category: Gurzhiy VV]] | |||
[[Category: Kasatsky PS]] | |||
[[Category: Konevega AL]] | |||
[[Category: Korban SA]] | |||
[[Category: Paleskava AV]] | |||
[[Category: Spiridonova ZA]] | |||
[[Category: Vinogradova DS]] | |||