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2rif
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:2rif.png|left|200px]] | ||
| - | < | + | ==CBS domain protein PAE2072 from Pyrobaculum aerophilum complexed with AMP== |
| - | + | <StructureSection load='2rif' size='340' side='right'caption='[[2rif]], [[Resolution|resolution]] 2.35Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[2rif]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RIF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RIF FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CS:CESIUM+ION'>CS</scene></td></tr> | |
| - | -- | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2rih|2rih]]</div></td></tr> |
| - | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PAE2072 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13773 Pyrobaculum aerophilum])</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=2rif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rif OCA], [https://pdbe.org/2rif PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rif RCSB], [https://www.ebi.ac.uk/pdbsum/2rif PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rif ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ri/2rif_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </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/main_output.php?pdb_ID=2rif ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cystathionine beta-synthase domains are found in a myriad of proteins from organisms across the tree of life and have been hypothesized to function as regulatory modules that sense the energy charge of cells. Here we characterize the structure and stability of PAE2072, a dimeric tandem cystathionine beta-synthase domain protein from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum. Crystal structures of the protein in unliganded and AMP-bound forms, determined at resolutions of 2.10 and 2.35 A, respectively, reveal remarkable conservation of key functional features seen in the gamma subunit of the eukaryotic AMP-activated protein kinase. The structures also confirm the presence of a suspected intermolecular disulfide bond between the two subunits that is shown to stabilize the protein. Our AMP-bound structure represents a first step in investigating the function of a large class of uncharacterized prokaryotic proteins. In addition, this work extends previous studies that have suggested that, in certain thermophilic microbes, disulfide bonds play a key role in stabilizing intracellular proteins and protein-protein complexes. | ||
| - | + | Structures and functional implications of an AMP-binding cystathionine beta-synthase domain protein from a hyperthermophilic archaeon.,King NP, Lee TM, Sawaya MR, Cascio D, Yeates TO J Mol Biol. 2008 Jun 27;380(1):181-92. Epub 2008 May 7. PMID:18513746<ref>PMID:18513746</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2rif" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Large Structures]] |
| - | + | ||
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Pyrobaculum aerophilum]] | [[Category: Pyrobaculum aerophilum]] | ||
| - | [[Category: Cascio, D | + | [[Category: Cascio, D]] |
| - | [[Category: King, N P | + | [[Category: King, N P]] |
| - | [[Category: Lee, T M | + | [[Category: Lee, T M]] |
| - | [[Category: Sawaya, M R | + | [[Category: Sawaya, M R]] |
| - | [[Category: Yeates, T O | + | [[Category: Yeates, T O]] |
[[Category: Amp binding protein]] | [[Category: Amp binding protein]] | ||
[[Category: Bateman domain]] | [[Category: Bateman domain]] | ||
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[[Category: Ligand-binding protein]] | [[Category: Ligand-binding protein]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 04:53:39 2009'' | ||
Current revision
CBS domain protein PAE2072 from Pyrobaculum aerophilum complexed with AMP
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