1th8: Difference between revisions

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 ==Crystal Structures of the ADP and ATP bound forms of the Bacillus Anti-sigma factor SpoIIAB in complex with the Anti-anti-sigma SpoIIAA: inhibitory complex with ADP, crystal form II==
-<StructureSection load='1th8' size='340' side='right' caption='[[1th8]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='1th8' size='340' side='right'caption='[[1th8]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1th8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TH8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TH8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1th8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TH8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TH8 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1thn|1thn]], [[1tid|1tid]], [[1til|1til]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPOIIAB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980]), SPOIIAA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980])</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=1th8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1th8 OCA], [https://pdbe.org/1th8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1th8 RCSB], [https://www.ebi.ac.uk/pdbsum/1th8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1th8 ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </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=1th8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1th8 OCA], [http://pdbe.org/1th8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1th8 RCSB], [http://www.ebi.ac.uk/pdbsum/1th8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1th8 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SP2AB_GEOSE SP2AB_GEOSE]] Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition.[HAMAP-Rule:MF_00637] [[http://www.uniprot.org/uniprot/SP2AA_GEOSE SP2AA_GEOSE]] In the phosphorylated form it could act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma f from inhibition.
+[https://www.uniprot.org/uniprot/SP2AB_GEOSE SP2AB_GEOSE] Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition.[HAMAP-Rule:MF_00637]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 32: @@
 ==See Also==
 *[[Anti-sigma factor antagonist|Anti-sigma factor antagonist]]
+*[[Anti-sigma factor antagonist 3D structures|Anti-sigma factor antagonist 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 12980]]
+[[Category: Geobacillus stearothermophilus]]
-[[Category: Transferase]]
+[[Category: Large Structures]]
-[[Category: Campbell, E A]]
+[[Category: Campbell EA]]
-[[Category: Darst, S A]]
+[[Category: Darst SA]]
-[[Category: Donigian, J]]
+[[Category: Donigian J]]
-[[Category: Leon, F]]
+[[Category: Leon F]]
-[[Category: Masuda, S]]
+[[Category: Masuda S]]
-[[Category: Murakami, K S]]
+[[Category: Murakami KS]]
-[[Category: Olson, C A]]
+[[Category: Olson CA]]
-[[Category: Wang, S]]
+[[Category: Wang S]]
-[[Category: Anti-anti-sigma]]
-[[Category: Anti-sigma]]
-[[Category: Serine kinase]]
-[[Category: Spoiiaa]]
-[[Category: Spoiiab]]
-[[Category: Sporulation]]
-[[Category: Transcription]]